Polypeptides that bind HIV gp120 and related nucleic acids, antibodies, compositions, and methods of use

ABSTRACT

The present invention provides, among other things, a polypeptide that binds with the gp120 envelope protein of HIV, in particular HIV-1, under physiological conditions, a nucleic acid that encodes such a polypeptide and can be expressed in a cell, a composition comprising such a polypeptide or nucleic acid or an antibody and a carrier therefor, a composition comprising a solid support matrix to which is attached an above-described polypeptide or an anti-antibody to a specified polypeptide sequence, a method of making an antibody to gp120, and a method of removing HIV from a bodily fluid.

TECHNICAL FIELD OF THE INVENTION

[0001] The present invention relates to polypeptides with homology toregions of domains of the human chemokine receptors CCR5, CXCR4, andSTRL33, as well as domains of CD4 that bind with human immunodeficiencyvirus (HIV), in particular HIV-1 glycoprotein 120 (gp120) envelopeprotein. The present invention also relates to nucleic acids encodingsuch polypeptides, antibodies, compositions comprising suchpolypeptides, nucleic acids or antibodies,,and methods of using thesame.

BACKGROUND OF THE INVENTION

[0002] There are seven transmembrane chemokine receptors that act ascofactors for HIV infection. The cofactors enable entry of HIV-1 intoCD4⁺T cells and macrophages (Premack et al., Nature Medicine 2: 1174-78(1996); and Zhang et al., Nature 383: 768 (1996)).

[0003] The presence of chemokines has an inhibitory effect on HIV-1attachment to, and infection of, susceptible cells. Additionally, somemutations in chemokine receptors have been shown to result in resistanceto HIV-1 infection. For example, a 32-nucleotide deletion within theCCR5 gene has been described in subjects who remained uninfected despiterepeated exposures to HIV-1 (Huang et al., Nature Medicine 2: 1240-43(1996)).

[0004] Evidence also exists for the physical association of a ternarycomplex between chemokine receptors, CD4, and HIV-1 gp120 envelopeglycoprotein on cell membranes (Lapham et al., Science 274: 602-05(1996)). Receptor signaling and cell activation are probably notrequired for the anti-HIV-1 effect of chemokines since a RANTES analoglacking the first eight amino-terminal amino acids, RANTES (9-68),lacked chemotactic and leukocyte-activating properties, but bound tomultiple chemokine receptors and inhibited infection bymacrophage-tropic HIV-1 (Arenzana-Seladedos et al., Nature 383: 400(1996)). Cumulatively, the above described results suggest that theinteraction between gp120, CD4, and at least one chemokine receptor isobligatory for HIV-1 infection. Accordingly, reagents that interferewith the binding of gp120 to chemokine receptors and to CD4 are used inthe biological and medical arts. However, there presently exists a needfor additional reagents that can compete with one or more proteins ofthe gp120-CD4-chemokine receptor complex to assist in basic biologicalor viral research, and to assist in medical intervention in the HIV-1pandemic. It is an object of the present invention to provide suchreagents. This and other objects and advantages, including additionalinventive features, will be apparent from the description providedherein.

BRIEF SUMMARY OF THE INVENTION

[0005] The present invention provides a polypeptide that binds with HIVgp120 under physiological conditions. Multiple embodiments of thepresent inventive polypeptide are provided, and each embodimentpossesses a degree of homology to at least one of the human CCR5, CXCR4and STRL33 chemokine receptors, and the human CD4 cell-surface protein.

[0006] In a first embodiment, the present invention provides apolypeptide comprising the amino acid sequence YDIXYYXXE, wherein X isany synthetic or naturally occurring amino acid residue, and thepolypeptide comprises less than about 100 contiguous amino acids thatare identical to, or, in the alternative, substantially identical to,the amino acid sequence of the human CCR5 chemokine receptor. Apreferred polypeptide of this first embodiment comprises the amino acidsequence YDIN*YYT*S*E. A more preferred polypeptide of this firstembodiment comprises the amino acid sequence YDINYYTSE, wherein eachletter is the standard one-letter abbreviation for an amino acid residue(i.e., for example, N denotes asparaginyl, T denotyes threoninyl, and Sdenotes serinyl). The polypeptide of the first embodiment can comprisethe amino acid sequence M*D*YQ*V*S*SP*IYDIN*YYT*S*E. Preferably, thepolypeptide comprises the amino acid sequence MDYQVSSPIYDINYYTSE.

[0007] In a second embodiment, the present invention provides apolypeptide comprising the amino acid sequence XEXIXIYXXXNYXXX, whereinX is any synthetic or naturally occurring amino acid and wherein saidpolypeptide comprises less than about 100 contiguous amino acid that areidentical to or substantially identical to the amino acid sequence ofthe human CXCR4 chemokine receptor. The polypeptide can consistessentially of, or consist of, the sequence EXIXIYXXXNY. Preferably, thepolypeptide comprises the sequence M*EG*IS*IYT*S*D*NYT*E*E*. Preferably,M*EG*IS*IYT*S*D*NYT*E*E* is M*EGISIYTSDNYT*E*E*.

[0008] In a third embodiment, the present invention provides apolypeptide comprising the amino acid sequence EHQAFLQFS, wherein saidpolypeptide comprises less than about 100 contiguous amino acids thatare identical to or substantially identical to the amino acid sequenceof the human STRL33 chemokine receptor. The polypeptide can consistessentially of, or consist of, the sequence EHQAFLQFS.

[0009] In a fourth embodiment, the present invention provides apolypeptide comprising at least a portion of an amino acid sequenceselected from the group consisting of LPPLYSLVFIFGFVGNML,QWDFGNTMCQLLTGLYFIGFFS, SQYQFWKNFQTLKIVILG, APYNIVLLLNTFQEFFGLNNCS, andYAFVGEKFRNYLLVFFQK, wherein said polypeptide comprises less than about100 contiguous amino acids that are identical to or substantiallyidentical to the amino acid sequence of the human CCR5 chemokinereceptor.

[0010] In a fifth embodiment, the present invention provides apolypeptide comprising at least a portion of an amino acid sequenceselected from the group consisting of LLLTIPDFIFANVSEADD,VVFQFQHIMVGLILPGIV, and IDSFILLEIIKQGCEFEN, wherein said polypeptidecomprises less than about 100 contiguous amino acids that are identicalto or substantially identical to the amino acid sequence of the humanCXCR4 chemokine receptor.

[0011] In a sixth embodiment, the present invention provides apolypeptide comprising at least a portion of an amino acid sequenceselected from the group consisting of LVISIFYHKLQSLTDVFL,PFWAYAGIHEWVFGQVMC, EAISTVVLATQMTLGFFL, LTMIVCYSVIIKTLLHAG,MAVFLLTQMPFNLMKFIRSTHW, HWEYYAMTSFHYTIMVTE, ACLNPVLYAFVSLKFRKN andSKTFSASHNVEATSMFQL, wherein said polypeptide comprises less than about100 contiguous amino acids that are identical to or substantiallyidentical to the amino acid sequence of the human STRL33 chemokinereceptor.

[0012] In a seventh embodiment, the present invention provides apolypeptide comprising at least a portion of an amino acid sequenceselected from the group consisting of DTYICEVED, EEVQLLVFGLTANSD,THLLQGQSLTLTLES, and GEQVEFSFPLAFTVE, wherein said polypeptide comprisesless than about 100 contiguous amino acids that are identical to orsubstantially identical to the amino acid sequence of the human CD4cell-surface protein.

[0013] In the fourth to seventh embodiments, any selected portion of thepolypeptide can comprise from 1 to about 6 conservative amino acidsubstitutions. In an alternative, the polypeptide can be partiallydefined by an absence of a polypeptide sequence, outside the region ofthe portion selected from the foregoing sequences, that has five, orten, contiguous amino acid residues that have a sequence that consistsof an amino acid sequence that is identical to or substantiallyidentical to the protein to which the polypeptide has homology (i.e.,CCR5, CXCR4, STRL33, or CD4). In yet another alternative, thepolypeptide can lack a sequence of five or ten contiguous amino acidswhich are identical to or substantially identical to the sequence of theprotein with which the sequence has homology except that one or moreconservatively or neutrally substituted amino acids replace part of thesequence of the protein to which the polypeptide has homology.Additionally, any embodiment of the present inventive polypeptide canalso comprise a pharmaceutically acceptable substituent.

[0014] Any embodiment of the present inventive polypeptide can beincorporated into a composition, which further comprises a carrier. Anysuitable embodiment of the present inventive polypeptide can be encodedby a nucleic acid that can be expressed in a cell. In this regard, thepresent invention further provides a vector comprising such a nucleicacid. The nucleic acids and vectors also can be incorporated into acomposition comprising a carrier.

[0015] Additionally, the present invention provides a method of makingan antibody to a polypeptide of the present invention. The presentinvention also provides a method of prophylactically or therapeuticallytreating an HIV infection in a mammal.

[0016] Additionally, the present invention provides an anti-idiotypicantibody comprising an internal image of a portion of gp120, as well asa method of selecting such an antibody.

[0017] The present invention also provides a method of making anantibody to a portion of the gp120 protein that binds with a portion ofCCR5, CXCR4, STRL33, or CD4, as well as the immunizing compound used tomake the antibody, and the antibody itself. In another embodiment of thepresent invention, a method of removing HIV-1 from a bodily fluid isprovided.

BRIEF DESCRIPTION OF THE DRAWINGS

[0018]FIG. 1 depicts a listing of synthetic amino acids available (fromBachem, King of Prussia, Pa.) for incorporation into polypeptides of thepresent invention.

DETAILED DESCRIPTION OF THE INVENTION

[0019] The present invention provides a polypeptide that binds withgp120 of HIV, in particular HIV-1, more particularly HIV-1_(LAI), underphysiological conditions. The polypeptide has a number of usesincluding, but not limited to, the use of the polypeptide to elucidatethe mechanism by which HIV, such as HIV-1, attaches to and/or infects aparticular cell, to induce an immune response in a mammal, in particulara human, to HIV, in particular HIV-1, and to inhibit the replication ofHIV, in particular HIV-1, in an infected mammal, in particular aMultiple embodiments of the present inventive polypeptide are provided.Each embodiment of the polypeptide has a degree of homology to at leastone of the human CCR5, CXCR4 and STRL33 chemokine receptors, or thehuman CD4 cell-surface protein. In each embodiment provided herein, aletter indicates the standard amino acid designated by that letter, anda letter followed directly by an asterisk (*) preferably represents theamino acid represented by the letter (e.g., N represents asparaginyl andT represents threoninyl), or a synthetic or naturally occurringconservative or neutral substitution therefor. Additionally, inaccordance with convention, all amino acid sequences provided herein aregiven either from left to right, or top to bottom, such that the firstamino acid is amino-terminal and the last is carboxyl-terminal. Thesynthesis of polypeptides, either synthetically (i.e., chemically) orbiologically, is within the skill in the art.

[0020] It is within the skill of the ordinary artisan to selectsynthetic and naturally occurring amino acids that make conservative orneutral substitutions for any particular naturally occurring aminoacids. The skilled artisan desirably will consider the context in whichany particular amino acid substitution is made in addition toconsidering the hydrophobicity or polarity of the side-chain, thegeneral size of the side chain, and the pK value of side-chains withacidic or basic character under physiological conditions. For example,lysine, arginine, and histidine are often suitably substituted for eachother, and more often arginine and lysine. As is known in the art, thisis because all three amino acids have basic side chains, whereas the pKvalue for the side-chains of lysine and arginine are much closer toeach-other (about 10 and 12) than to histidine (about 6). Similarly,glycine, alanine, valine, leucine, and isoleucine are often suitablysubstituted for each other, with the proviso that glycine is frequentlynot suitably substituted for the other members of the group. This isbecause each of these amino acids are relatively hydrophobic whenincorporated into a polypeptide, but glycine's lack of an α-carbonallows the phi and psi angles of rotation (around the α-carbon) so muchconformational freedom that glycinyl residues can trigger changes inconformation or secondary structure that do not often occur when theother amino acids are substituted for each other. Other groups of aminoacids frequently suitably substituted for each other include, but arenot limited to, the group consisting of glutamic and aspartic acids; thegroup consisting of phenylalanine, tyrosine and tryptophan; and thegroup consisting of serine, threonine and, optionally, tyrosine.Additionally, the skilled artisan can readily group synthetic aminoacids with naturally occurring amino acids.

[0021] In the context of the present invention, a polypeptide is“substantially identical” to another polypeptide if it comprises atleast about 80% identical amino acids. Desirably, at least about 50% ofthe non-identical amino acids are conservative or neutral substitutions.Also, desirably, the polypeptides differ in length (i.e., due todeletion mutations) by no more than about 10%.

[0022] In a first embodiment, the present invention provides apolypeptide comprising the amino acid sequence YDIXYYXXE, wherein X isany synthetic or naturally occurring amino acid residue, and thepolypeptide comprises less than about 100 contiguous amino acids,preferably less than about 50 amino acids, more preferably less thanabout 25 amino acids, and yet more preferably less than about 13 aminoacids that are identical to, or, in the alternative, substantiallyidentical to, the amino acid sequence of the human CCR5 chemokinereceptor.

[0023] Preferably, the polypeptide of the first embodiment comprisesYDIXYYXXE, wherein the amino moiety of the amino-terminal tyrosinylresidue is not bound to another amino acid residue via a peptidic bond,and the carboxyl moiety of the glutamyl residue is not bound to anotheramino acid residue via a peptidic bond. However, the polypeptide canconsist essentially of YDIXYYXXE and, optionally, can be modified by oneor more pharmaceutically acceptable substituents, such as, for example,t-boc or a saccharide.

[0024] More particularly, the polypeptide comprises the amino acidsequence YDIN*YYT*S*E. Preferably, N* is asparaginyl, T* is threoninyl,and S* is serinyl.

[0025] The polypeptide of the first embodiment can comprise adodecapeptide selected from the amino acid sequenceM*D*YQ*V*S*SP*IYDIN*YYT*S*E. More preferably, the polypeptide of thefirst embodiment comprises the amino acid sequence MDYQVSSPIYDINYYTSE.

[0026] In a second embodiment, the present invention provides apolypeptide comprising the amino acid sequence XEXIXIYXXXNYXXX, whereinX is any synthetic or naturally occurring amino acid, and thepolypeptide comprises less than about 100 contiguous amino acids,preferably less than about 50 amino acids, and more preferably less thanabout 25 amino acids, that are identical to or substantially identicalto the amino acid sequence of the human CXCR4 chemokine receptor.Optionally, the polypeptide consists essentially of, or consists of, thesequence EXIXIYXXXNY.

[0027] In a preferred polypeptide of this second embodiment, thepolypeptide comprises the amino acid sequence M*EG*IS*IYT*S*i*NYT*E*E*.Preferably, M*EG*IS*IYT*S*D*NYT*E*E* is M*EGISIYTSDNYT*E*E*.

[0028] In a third embodiment, the present invention provides apolypeptide comprising the amino acid sequence EHQAFLQFS, wherein thepolypeptide comprises less than about 100 contiguous amino acidresidues, preferably less than about 50 contiguous amino acid residues,more preferably less than about 25 contiguous amino acid residues, thatare identical to or substantially identical to the amino acid sequenceof the human STRL33 chemokine receptor. The polypeptide can consistessentially of, or consist of, the sequence EHQAFLQFS.

[0029] The first three embodiments of the present invention provide,among other things, polypeptides having substantial identity or identityto the amino-terminal regions of the chemokine receptors CCR5, CXCR4,and STRL33. These first three embodiments form a first group ofembodiments of the present invention. The present invention alsoprovides, in a second group of embodiments, polypeptides havingsubstantial identity or identity to an internal region of the humanchemokine receptors CCR5, CXCR4, and STRL33, as well as to the leukocytecell-surface protein CD4.

[0030] This second group of embodiments provides a polypeptide thatbinds with HIV gp120 under physiological conditions and comprises atleast a portion of or all of an amino acid sequence selected from thegroup consisting of LPPLYSLVFIFGFVGNML, QWDFGNTMCQLLTGLYFIGFFS,SQYQFWKNFQTLKIVILG, APYNIVLLLNTFQEFFGLNNCS, and YAFVGEKFRNYLLVFFQK,wherein the polypeptide comprises less than about 100 amino acids thatare identical to or substantially identical to the amino acid sequenceof the human CCR5 chemokine receptor; or selected from the groupconsisting of LLLTIPDFIFANVSEADD (165-182), VVFQFQHIMVGLILPGIV(197-214), and IDSFILLEIIKQGCEFEN (261-278), wherein the polypeptidecomprises less than about 100 amino acids that are identical to orsubstantially identical to the amino acid sequence of the human CXCR4chemokine receptor; or

[0031] selected from the group consisting of LVISIFYHKLQSLTDVFL (53-70),PFWAYAGIHEWVFGQVMC (85-102), EAISTVVLATQMTLGFFL (185-202),LTMIVCYSVIIKTLLHAG (205-222), MAVFLLTQMPFNIMKFIRSTHW (237-258),HMEYYAMTSFHYTIMVTE (257-274), ACLNPVLYAFVSLKFRKN (281-298) andSKTFSASHEATSMFQL (325-342), wherein the polypeptide comprises less thanabout 100 amino acids that are identical to a substantially identical tothe amino acid sequence of the human STRL33 chemokine receptor; or

[0032] selected from the group consisting of DTYICEVED, EEVQLLVFGLTANSD,THLLQGQSLTLTLES, and GEQVEFSFPLAFTVE, wherein the polypeptide binds withHIV gp120 under physiological conditions and comprises less than about100 amino acids that are identical to or substantially identical to theamino acid sequence of the human CD4 cell-surface protein. Optionally,the recited amino acid sequences can comprise 1 to about 6 conservativeor neutral amino acid substitutions.

[0033] The polypeptides of this second group of embodiments preferablycomprise less than about 50 amino acid residues, and more preferablyless than about 25 amino acid residues, and yet more preferably noadditional amino acid residues, that are identical to a protein thatnaturally has the recited amino acid sequence. The polypeptide can bealternatively characterized by an absence of a region, outside theabove-recited amino acid sequences, that has about five, or about ten,contiguous amino acid residues that have a sequence that consists of anamino identical and conservatively substituted residues as an amino acidsequence of the protein to which the polypeptide of the compound hashomology.

[0034] Any embodiment of the present inventive polypeptide can alsocomprise a pharmaceutically acceptable substituent, attachment of whichis within the skill in the art. The pharmaceutically acceptability ofsubstituents are understood by those skilled in the art. For example, apharmaceutically acceptable substituent can be a biopolymer, such as apolypeptide, an RNA, a DNA, or a polysaccharide. Suitable polypeptidescomprise fusion proteins, an antibody or fragment thereof, a celladhesion molecule or a fragment thereof, or a peptide hormone. Suitablepolysaccharides comprise polyglucose moieties, such as starch and theirderivatives, such as heparin. The pharmaceutically acceptablesubstituent also can be any suitable lipid or lipid-containing moiety,such as a lipid of a liposome or a vesicle, or even a lipophilic moiety,such as a prostaglandin, a steroid hormone, or a derivative thereof.Additionally, the pharmaceutically acceptable substituent can be anucleotide or nucleoside, such as nicotine adenine dinucleotide orthymine, an amino acid residue, a saccharide or disaccharide, or theresidue of another biomolecule naturally occurring in a cell, such asinositol, a vitamin, such as vitamin C, thiamine, or nicotinic acid.Synthetic organic moieties also can be pharmaceutically acceptablesubstituents, such as t-butyl carbonyl, an acetyl moiety, quinine,polystyrene and other biologically acceptable polymers. Optionally, apharmaceutically acceptable substituent can be selected from the groupconsisting of a C₁-C₁₈ alkyl, a C₂-C₁₈ alkenyl, a C₂-C₁₈ alkynyl, aC₆-C₁₈ aryl, a C₇-C₁₈ alkaryl, a C₇-C₁₈ aralkyl, and a C₃-C₁₈cycloalkyl, wherein any of the foregoing moieties that are cycliccomprise from 0 to 2 atoms per carbocyclic ring, which can be the sameor different, and are selected from the group consisting of nitrogen,oxygen, and sulfur.

[0035] Any of the substituents from this group can be substituted by oneto six substituent moieties, which can be the same or different,selected from the group consisting of an amino moiety, a carbamatemoiety, a carbonate moiety, hydroxyl, a phosphamate moiety, a phosphatemoiety, a phosphonate moiety, a pyrophosphate moiety, a triphosphatemoiety, a sulfamate moiety, a sulfate moiety,, a sulfonate moiety, aC₁-C₈ monoalkylamine moiety, a C₁-C₈ dialkylamine moiety, and a C₁-C₈trialkylamine moiety.

[0036] Any embodiment of the present inventive polypeptide can beencoded by a nucleic acid and can be expressed in a cell. The skilledartisan will recognize that the encoded polypeptide as well as anypharmaceutically acceptable substituent to be incorporated into thepolypeptide, e.g., a formyl or acetyl substituent on an amino-terminalmethionine or a saccharide, will preferably be produced by a cell thatcan express the polypeptide of the present invention. Accordingly, theamino acids incorporated into the polypeptide encoded by the nucleicacid are preferably naturally occurring.

[0037] A nucleic acid as described above can be cloned into any suitablevector and can be used to transduce, transform, or transfect anysuitable host. The selection of vectors and methods to construct themare commonly known to persons of ordinary skill in the art and aredescribed in general technical references (see, in general, “RecombinantDNA Part D,” Methods in Enzymology, Vol. 153, Wu and Grossman, eds.,Academic Press (1987)). Desirably, the vector comprises regulatorysequences, such as transcription and translation initiation andtermination codons, which are specific to the type of host (e.g.,bacterium, fungus, plant, or animal) into which the vector is to beinserted, as appropriate and taking into consideration whether thevector is DNA or RNA. Preferably, the vector comprises regulatorysequences that are specific to the genus of the host. Most preferably,the vector comprises regulatory sequences that are specific to thespecies of the host and is optimized for the expression of anabove-described polypeptide.

[0038] Constructs of vectors, which are circular or linear, can beprepared to contain an entire nucleic acid sequence as described aboveor a portion thereof ligated to a replication system that is functionalin a prokaryotic or eukaryotic host cell. Replication systems can bederived from ColE1, 2 mμ plasmid, λ, SV40, bovine papilloma virus, andthe like.

[0039] Suitable vectors include those designed for propagation andexpansion, or for expression, or both. A preferred cloning vector isselected from the group consisting of the pUC series, the pBluescriptseries (Stratagene, LaJolla, Calif.), the pET series (Novagen, Madison,Wis.), the pGEX series (Pharmacia Biotech, Uppsala, Sweden), and the pEXseries (Clonetech, Palo Alto, Calif.). Examples of animal expressionvectors include pEUK-C1, pMAM and pMAMneo (Clonetech, Palo Alto,Calif.).

[0040] An expression vector can comprise a native or nonnative promoteroperably linked to a nucleic acid molecule encoding an above-describedpolypeptide. The selection of promoters, e.g., strong, weak, inducible,tissue-specific and developmental-specific, is within the skill in theart. Similarly, the combining of a nucleic acid molecule as describedabove with a promoter is also within the skill in the art.

[0041] The skilled artisan will also recognize that the polypeptide hasability to bind the gp120 protein, which is most often found outside ofcells. Accordingly, the present inventive nucleic acid advantageouslycan comprise a nucleic acid sequence that encodes a signal sequence suchthat a signal sequence is translated as a fusion protein with thepolypeptide of the present inventive polypeptide to form a signalsequence-polypeptide fusion. The signal sequence can cause secretion ofthe entire polypeptide, including the signal sequence (which is apharmaceutically acceptable substituent), or can be cleaved from thepolypeptide (i.e., the polypeptide of the compound) prior to, or during,secretion so that at least the present inventive polypeptide is secretedout of a cell in which the nucleic acid is expressed.

[0042] Alternatively, the nucleic acid comprises or encodes an antisensenucleic acid molecule or a ribozyme that is specific for a specifiedamino acid sequence of an above-described polypeptide. A nucleic acidsequence introduced in antisense suppression generally is substantiallyidentical to at least a portion of the endogenous gene or gene to berepressed, but need not be identical. Thus, the vectors can be designedsuch that the inhibitory effect applies to other proteins within afamily of genes exhibiting homology or substantial homology to thetarget gene. The introduced sequence also need not be full-lengthrelative to either of the primary transcription product or the fullyprocessed mRNA. Generally, higher homology can be used to compensate forthe use of a shorter sequence. Furthermore, the introduced sequence neednot have the same intron or exon pattern, and homology of non-codingsegments will be equally effective.

[0043] Ribozymes also have been reported to have use as a means toinhibit expression of endogenous genes. It is possible to designribozymes that specifically pair with virtually any target RNA andcleave the phosphodiester backbone at a specific location, therebyfunctionally inactivating the target RNA. In carrying out this cleavage,the ribozyme is not itself altered and is, thus, capable of recyclingand cleaving other molecules, making it a true enzyme. The inclusion ofribozyme sequences within antisense RNAs confers RNA-cleaving activityupon them, thereby increasing the activity of the constructs. The designand use of target RNA-specific ribozymes is described in Haseloff etal., Nature 334: 585-591 (1988).

[0044] Further provided by the present invention is a compositioncomprising an above-described polypeptide or nucleic acid and a carriertherefor. Another composition provided by the present invention is acomposition comprising an antibody to an above-described polypeptide oran anti-antibody to an above-described polypeptide.

[0045] Any embodiment of the present invention including the presentinventive polypeptide, nucleic acid, antibody, and anti-antibody, can beincorporated into a composition comprising a carrier. The carrier canserve any function. For example, the carrier can increase the solubilityof the present inventive polypeptide, nucleic acid or antibody inaqueous solutions. Additionally, the carrier can protect the presentinventive polypeptide, nucleic acid or antibody from environmentalinsults, such as dehydration, oxidation, and photolysis. Moreover, thecarrier can serve as an adjuvant, or as a timed-release control means ina biological system.

[0046] Antibodies can be generated in accordance with methods known inthe art. See, for example, Benjamin, In Immnunology: a short course,Wiley-Liss, NY, 1996, pp. 436-437; Kuby, In Immunology, 3rd. ed.,Freeman, NY, 1997, pp. 455-456; Greenspan et al., FASEB J. 7: 437-443(1993); and Poskitt, Vaccine 9: 792-796 (1991). Anti-antibodies (i.e.,anti-idiotypic antibodies) also can be generated in accordance withmethods known in the art (see, for example, Benjamin, In Immunology: ashort course, Wiley-Liss, NY, 1996, pp. 436-437; Kuby, In Immunology,3rd. ed., Freeman, NY, 1997, pp. 455-456; Greenspan et al., FASEB J., 7,437-443, 1993; Poskitt, Vaccine, 9, 792-796, 1991; and Madiyalakan etal., Hybridonor 14: 199-203 (1995) (“Anti-idiotype induction therapy”)).Such antibodies can be obtained and employed either in solution-phase orcoupled to a desired solid-phase matrix. Having in hand such antibodies,one skilled in the art will further appreciate that such antibodies,using well-established procedures (e.g., such as described by Harlow andLane (1988, supra), are useful in the detection, quantification, orpurification of gp120 or HIV, particularly HIV-1, conjugates of each andhost cells transformed to produce a gp120 receptor or a derivativethereof. Such antibodies are also useful in a method of prevention ortreatment of a viral infection and in a method of inducing an immuneresponse to HIV as provided herein.

[0047] In view of the above, an above-described polypeptide can beadministered to an animal. The animal generates anti-polypeptideantibodies. Among the anti-polypeptide antibodies generated or inducedin the animal are antibodies that have an internal image of gp120. Inaccordance with well-known methods, polyclonal or monoclonal antibodiescan be obtained, isolated and selected. Selection of an anti-polypeptideantibody that has an internal image of gp120 can be based uponcompetition between the anti-polypeptide antibody and gp120 for bindingto an above-described polypeptide, or upon the ability of theanti-polypeptide antibody to bind to a free polypeptide as opposed to apolypeptide bound to gp120. Such an anti-antibody can be administered toan animal to prevent or treat an HIV infection in accordance withmethods provided herein.

[0048] Although nonhuman anti-idiotypic antibodies, such as ananti-polypeptide antibody that has an internal image of gp120 and,therefore, is anti-idiotypic to gp120, are useful for prophylaxis inhumans, their favorable properties might, in certain instances, can befurther enhanced and/or their adverse properties further diminished,through “humanization” strategies, such as those recently reviewed byVaughan, Nature Biotech., 16, 535-539, 1998.

[0049] Prior to administration to an animal, such as a mammal, inparticular a human, an above-described polypeptide, nucleic acid,antibody or anti-antibody can be formulated into various compositions bycombination with appropriate carriers, in particular, pharmaceuticallyacceptable carriers or diluents, and can be formulated to be appropriatefor either human or veterinary applications.

[0050] The present invention also provides a method of making anantibody. The method comprises administering an immunogenic amount of anabove-described polypeptide or nucleic acid to an animal, such as amammal, in particular a human. Determining the quantity of a polypeptideor nucleic acid that is immunogenic will depend in part on the degree ofsimilarity to a protein or other molecule of the inoculated animal, theroute of administration of the polypeptide or nucleic acid, and the sizeof the polypeptide administered or encoded by the administered nucleicacid. If necessary, the polypeptide or nucleic acid can be mixed with orligated to a substance (or an adjuvant) that enhances itsimmunogenicity. Such calculations and procedures are within the skill ofthe ordinary artisan. Additionally, the present inventive methodpreferably can be used to induce an immune response against HIV,particularly HIV-1, in a mammal, particularly a human.

[0051] In view of the above, the present invention further provides amethod of prophylactically or therapeutically treating an HIV infectionin a mammal, particularly a human, in need thereof. The method comprisesadministering to the mammal an HIV replication-inhibiting effectiveamount of an above-described polypeptide, nucleic-acid, or ananti-antibody to an above-described polypeptide or a nucleic acidencoding such a polypeptide.

[0052] The present invention also provides a method of prophylacticallyor therapeutically treating HIV infection in a mammal. The methodcomprises administering to the mammal an effective amount of anabove-described polypeptide or nucleic acid. Prior to administration toan animal, such as a mammal, in particular a human, an above-describedpolypeptide or nucleic acid can be formulated into various compositionsby combination with appropriate carriers, in particular,pharmaceutically acceptable carriers or diluents, and can be formulatedto be appropriate for either human or veterinary applications.

[0053] Thus, a composition for use in the method of the presentinvention can comprise one or more of the polypeptides, nucleic acids,antibodies or anti-antibodies described herein, preferably incombination with a pharmaceutically acceptable carrier. Pharmaceuticallyacceptable carriers are well-known to those skilled in the art, as aresuitable methods of administration. The choice of carrier will bedetermined, in part, by whether a polypeptide or a nucleic acid is to beadministered, as well as by the particular method used to administer thecomposition. Optionally, the carrier can be selected to increase thesolubility of the composition or mixture, e.g., a liposome orpolysaccharide. One skilled in the art will also appreciate that variousroutes of administering a composition are available, and, although morethan one route can be used for administration, a particular route canprovide a more immediate and more effective reaction than another route.Accordingly, there are a wide variety of suitable formulations ofcompositions that can be used in the present inventive methods.

[0054] A composition in accordance with the present invention, alone orin further combination with one or more other active agents, can be madeinto a formulation suitable for parenteral administration, preferablyintraperitoneal administration. Such a formulation can include aqueousand nonaqueous, isotonic sterile injection solutions, which can containantioxidants, buffers, bacteriostats, and solutes that render theformulation isotonic with the blood of the intended recipient, andaqueous and nonagueous sterile suspensions that can include suspendingagents, solubilizers, thickening agents, stabilizers, and preservatives.The formulations can be presented in unit dose or multi-dose sealedcontainers, such as ampules and vials, and can be stored in afreeze-dried (lyophilized) condition requiring only the addition of thesterile liquid carrier, for example, water, for injections, immediatelyprior to use. Extemporaneously injectable solutions and suspensions canbe prepared from sterile powders, granules, and tablets, as describedherein.

[0055] A formulation suitable for oral administration can consist ofliquid solutions, such as an effective amount of the compound dissolvedin diluents, such as water, saline, or fruit juice; capsules, sachets ortablets, each containing a predetermined amount of the activeingredient, as solid or granules; solutions or suspensions in an aqueousliquid; and oil-in-water emulsions or water-in-oil emulsions. Tabletforms can include one or more of lactose, mannitol, corn starch, potatostarch, microcrystalline cellulose, acacia, gelatin, colloidal silicondioxide, croscarmellose sodium, talc, magnesium stearate, stearic acid,and other excipients, colorants, diluents, buffering agents, moisteningagents, preservatives, flavoring agents, and pharmacologicallycompatible carriers.

[0056] Similarly, a formulation suitable for oral administration caninclude lozenge forms, which can comprise the active ingredient in aflavor, usually sucrose and acacia or tragacanth; pastilles comprisingthe active ingredient in an inert base, such as gelatin and glycerin, orsucrose and acacia; and mouthwashes comprising the active ingredient ina suitable liquid carrier; as well as creams, emulsions, gels, and thelike containing, in addition to the active ingredient, such carriers asare known in the art.

[0057] An aerosol formulation suitable for administration via inhalationalso can be made. The aerosol formulation can be placed into apressurized acceptable propellant, such as dichlorodifluoromethane,propane, nitrogen, and the like.

[0058] A formulation suitable for topical application can be in the formof creams, ointments, or lotions.

[0059] A formulation for rectal administration can be presented as asuppository with a suitable base comprising, for example, cocoa butteror a salicylate. A formulation suitable for vaginal administration canbe presented as a pessary, tampon, cream, gel, paste, foam, or sprayformula containing, in addition to the active ingredient, such carriersas are known in the art to be appropriate.

[0060] Important general considerations for design of delivery systemsand compositions, and for routes of administration, for polypeptidedrugs also apply (Eppstein, CRC Crit. Rev. Therapeutic Drug CarrierSystems 5, 99-139, 1988; Siddiqui et al., CRC Crit. Rev. TherapeuticDrug Carrier Systems 3, 195-208, 1987); Banga et al., Int. J.Pharmaceutics 48, 15-50, 1988; Sanders, Eur. J. Drug Metab.Pharmacokinetics 15, 95-102, 1990; Verhoef, Eur. J. Drug Metab.Pharmacokinetics 15, 83-93, 1990). The appropriate delivery system for agiven polypeptide will depend upon its particular nature, the particularclinical application, and the site of drug action. As with any proteindrug, oral delivery will likely present special problems, due primarilyto instability in the gastrointestinal tract and poor absorption andbioavailability of intact, bioactive drug therefrom. Therefore,especially in the case of oral delivery, but also possibly inconjunction with other routes of delivery, it will be necessary to usean absorption-enhancing agent in combination with a given polypeptide. Awide variety of absorption-enhancing agents have been investigatedand/or applied in combination with protein drugs for oral delivery andfor delivery by other routes (Verhoef, 1990, supra; van Hoogdalem,Pharmac. Ther. 44, 407-43, 1989; Davis, J. Pharm. Pharmacol. 44(Suppl.1), 186-90, 1992). Most commonly, typical enhancers fall into thegeneral categories of (a) chelators, such as EDTA, salicylates, andN-acyl derivatives of collagen, (b) surfactants, such as lauryl sulfateand polyoxyethylene-9-lauryl ether, (c) bile salts, such as glycholateand taurocholate, and derivatives, such as taurodihydrofusidate, (d)fatty acids, such as oleic acid and capric acid, and their derivatives,such as acylcarnitines, monoglycerides, and diglycerides, (e)non-surfactants, such as unsaturated cyclic ureas, (f) saponins, (g)cyclodextrins, and (h) phospholipids.

[0061] Other approaches to enhancing oral delivery of protein drugs caninclude the aforementioned chemical modifications to enhance stabilityto gastrointestinal enzymes and/or increased lipophilicity.Alternatively, the protein drug can be administered in combination withother drugs or substances that directly inhibit proteases and/or otherpotential sources of enzymatic degradation of proteins. Yet anotheralternative approach to prevent or delay gastrointestinal absorption ofprotein drugs is to incorporate them into a delivery system that isdesigned to protect the protein from contact with the proteolyticenzymes in the intestinal lumen and to release the intact protein onlyupon reaching an area favorable for its absorption. A more specificexample of this strategy is the use of biodegradable microcapsules ormicrospheres, both to protect vulnerable drugs from degradation, as wellas to effect a prolonged release of active drug (Deasy, inMicroencapsulation and Related Processes, Swarbrick, ed., MarcellDekker, Inc.: New York, 1984, pp. 1-60, 88-89, 208-11). Microcapsulesalso can provide a useful way to effect a prolonged delivery of aprotein drug after injection (Maulding, J. Controlled Release 6, 167-76,1987).

[0062] The dose administered to an animal, such as a mammal,particularly a human, in the context of the present invention should besufficient to effect a therapeutic or prophylactic response in theindividual over a reasonable time frame. The dose will be determined bythe particular polypeptide, nucleic acid, antibody, or anti-antibodyadministered, the severity of any existing disease state, as well as thebody weight and age of the individual. The size of the dose also will bedetermined by the existence of any adverse side effects that mayaccompany the use of the particular polypeptide, nucleic acid, antibodyor anti-antibody employed. It is always desirable, whenever possible, tokeep adverse side effects to a minimum.

[0063] The dosage can be in unit dosage form, such as a tablet orcapsule. The term “unit dosage form” as used herein refers to physicallydiscrete units suitable as unitary dosages for human and animalsubjects, each unit containing a predetermined quantity of a vector,alone or in combination with other active agents, calculated in anamount sufficient to produce the desired effect in association with apharmaceutically acceptable diluent, carrier, or vehicle. Thespecifications for the unit dosage forms of the present invention dependon the particular embodiment employed and the effect to be achieved, aswell as the pharmacodynamics associated with each polypeptide, nucleicacid or anti-antibody in the host. The dose administered should be an“HIV infection inhibiting amount” of an above-described polypeptide ornucleic acid or an “immune response-inducing effective amount” of anabove-described polypeptide, an above-described nucleic acid, or anantibody as appropriate.

[0064] Another composition provided by the present invention is acomposition comprising a solid support matrix to which is attached anabove-described polypeptide, or an anti-antibody to an above-describedpolypeptide. The solid matrix can comprise other functional reagentsincluding, for example, polyethylene glycol, dextran, albumin and thelike, whose intended effector functions may include one or more of thefollowing: to improve stability of the conjugate; to increase thehalf-life of the conjugate; to increase resistance of the conjugate toproteolysis; to decrease the immunogenicity of the conjugate; to providea means to attach or immobilize a functional polypeptide oranti-antibody onto a solid support matrix (e.g., see, for example,Harris, in Poly(Ethylene Glycol) Chemistry: Biotechnical and BiomedicalApplications, Harris, ed., Plenum Press: New York (1992), pp. 1-14).Conjugates furthermore may comprise a polypeptide or anti-antibodycoupled to an effector molecule, each of which, optionally, may havedifferent functions (e.g., such as a toxin molecule (or an immunologicalreagent) and a polyethylene glycol (or dextran or albumin) molecule).Diverse applications and uses of functional proteins and polypeptides,attached to or immobilized on a solid support matrix, are exemplifiedmore specifically for poly(ethylene glycol) conjugated proteins orpeptides in a review by Holmberg et al. (In Poly(Ethylene Glycol)Chemistry: Biotechnical and Biomedical Applications, Harris, ed., PlenumPress: New York, 1992, pp. 303-324).

[0065] In addition, the present invention provides a method of removingHIV from a bodily fluid of an animal. The method comprisesextracorporeally contacting the bodily fluid of the animal with asolid-support matrix to which is attached an above-described polypeptideor an anti-antibody to an above-described polypeptide. Alternatively,the bodily fluid can be contacted with the polypeptide or anti-antibodyin solution and then the solution can be contacted with a solid supportmatrix to which is attached a means to remove the polypeptide oranti-antibody to which is bound HIV gp120 from the bodily fluid.

[0066] Methods of attaching an herein-described polypeptide, or ananti-antibody to a solid support matrix are known in the art. “Attached”is used herein to refer to attachment to (or coupling to) andimmobilization in or on a solid support matrix. See, for example,Harris, in Poly(Ethylene Glycol) Chemistry: Biotechnical and BiomedicalApplications, Harris, ed., Plenum Press: New York (1992), pp. 1-14) andinternational patent application WO 91/02714 (Saxinger). Diverseapplications and uses of functional polypeptides attached to orimmobilized on a solid support matrix are exemplified more specificallyfor poly(ethylene glycol) conjugated proteins or peptides in a review byHolmberg et al. (In Poly(Ethylene Glycol) Chemistry: Biotechnical andBiomedical Applications, Harris, ed., Plenum Press: New York, 1992, pp.303-324).

[0067] The present invention also provides a method of making anantibody that binds to gp120 of HIV under physiological conditions. Themethod comprises labeling an embodiment of the present inventivecompound to obtain a labeled compound. Labeling compounds are within theskill of the ordinary artisan. For example, the present inventivecompound can be labeled with radioactive atom, such as ¹²⁵I in the sameor a similar manner as was performed in the examples provided below.Alternatively, an enzyme, such as horseradish peroxidase, can beattached to or incorporated into the present inventive compound. Then byexposing a chromogenic or photogenic compound to the compound, a signalindicative of the presence and quantity of the compound present can begenerated. In another alternative, a polyhistidinyl moiety can beattached to, or incorporated into, the present inventive moiety so thatthe present inventive compound will react with high affinity totransition metal ions such as nickel, copper, or zinc ions; thisreaction can be used as the basis to quantify the amount of the presentinventive compound present at a particular location. In yet anotheralternative, the present inventive compound can be used as antigen to astandard antibody that specifically recognizes an antigenic epitope ofthe present inventive compound. As is well-known, the standard antibodycan itself be labeled or used in conjunction with an additional antibodythat is labeled with an enzyme, radioisotope, or other suitable means.The skilled artisan will recognize that there is a plethora of othersuitable means and methods to label the present inventive compound.

[0068] This present inventive method of making an antibody that binds toa gp120 envelope protein of HIV further comprises providing a library ofsynthetic peptides. The library consists of a multiplicity ofsynthetically-produced polypeptides that are homologous, and preferablyessentially identical (i.e., having the same primary amino acid residuesequence, ignoring blocking groups, phosphorylation of serinyl,threoninyl, and tyrosinyl residues, hydroxylation of prolinyl residues,and the like) or identical, to a continuous region of an HIV gp120envelope protein. The polypeptides of the library can be any suitablelength. While larger regions allow faster scanning and tend to preservenon-linear epitopes, shorter length polypeptides allow more sensitivescreening of the primary sequence of the gp120 protein. However,polypeptides that are too short can lose essential secondary structureor cleave reactive sites into one or more pieces. Preferably, a mixtureof short and long polypeptides are incorporated into the library,however, the library can consist of polypeptides of a single length(measured in amino acid residues). For the sake of convenience thelibrary can be split into multiple parts, and screened by parts.Typically, the polypeptides of the library will be between about 6 andabout 45 amino acid residues in length.

[0069] Typically, the library will comprise a series of polypeptideseach having an identical sequence to that of gp120 but having anamino-terminus a particular number of amino acids downstream of theamino-terminus of the prior polypeptide (see, examples section below).The distance, measured in amino acid residues, is referred to as theoffset. Preferably, libraries that are characterized by the existence ofan offset, the offset is not greater than the product of length of thelongest polypeptide measured in amino acid residues and 1.5, preferably1.0, and more preferably 0.5. The library can be alternativelycharacterized by the existence of an offset not greater than 30,preferably 15, and more preferably 4.

[0070] Each polypeptide of the library is substantially isolated fromevery other polypeptide of said library and is located in a knownposition. For example, each polypeptide can be bound to a solid supportand that is in a vessel or that can be placed in a vessel. The vesselpreferably enables each polypeptide to be covered in a liquid that doesnot contact any other oligonucleotide of the library. By way of example,each polypeptide can be bound to a bead that is placed in a vessel (ortube) or can be bound to the well of a multi-well assay plate.Alternatively, an array of polypeptides can be fashioned, for example ona microchip device (as is presently used in some DNA sequencing devicesand methods), and the entire array can be bathed in a single solution.

[0071] Each polypeptide is then individually contacted with the labeledcompound such that a portion of the labeled compound can bind with thepolypeptide of the library. In this way, a bound population of eachlabeled compound of the present invention and an unbound population ofthe labeled compound is generated. The phrase individually contactedmeans that each polypeptide has the opportunity to bind with the labeledcompound and the quantity of labeled compound bound by each can bedetermined.

[0072] The method then comprises removing substantially all of theunbound labeled compound from the position occupied by each polypeptide.That is, the solution comprising the labeled compound is separated fromthe polypeptides of the library and the bound population of the labeledcompound. This can be done by any suitable method, e.g., by aspirationand one or more washing steps comprising adding a quantity of liquidsufficient to cover all the surfaces that were contacted by the labeledcompound and aspirating away substantially all of the wash liquid.

[0073] The amount of labeled compound that remains co-localized witheach polypeptide of the library is then measured to determine thequantity of labeled compound bound by each polypeptide. The amount ofthe present inventive compound bound by each polypeptide can be directlyevaluated to identify a portion of the HIV gp120 envelope protein thatbinds to an (HIV)-receptor selected from the group consisting of CCR5,CXCR4, STRL33, and CD4. This information is then used to identify andprovide an immunizing compound. The immunizing compound comprises apolypeptide comprising an amino acid sequence that is homologous to, orpreferably is essentially identical to, or identical to, the portion ofthe HIV-1 gp120 envelope protein that binds with CD4, CCR5, CXCR4,and/or STRL33. The immunizing protein can be provided by processinggp120, e.g., proteolytically digesting gp120 that has been isolated froma preparation of HIV-1. Preferably, however, the immunizing compound isprepared synthetically, or by genetic engineering, or by a combinationof genetic engineering and synthetic methods. The immunizing compoundcan comprise a pharmaceutically acceptable substituent, can be encodedby a nucleic acid that can be expressed in a cell, can be mixed with acarrier, and is an inventive aspect of the present invention.

[0074] An immunogenic quantity of the immunizing compound is theninserted into an animal (e.g., a human, or a rodent, a canine, a feline,or a ruminant) in a manner consistent with the discussion of a method ofraising an antibody to the present inventive compounds that arehomologous to portions of CCR5, CXCR4, STRL33, and CD4, above. Theinsertion of the immunizing compound causes the inoculated animal toproduce an antibody that binds with said portion of the HIV gp120envelope protein. Thus the present invention also provides an antibodythat binds to an HIV gp120 envelope protein, as well as an antigenbinding protein comprising one or more complementarity determiningregions of the antibody (e.g., a Fab, a Fab_(2′), an Fv, a single-chainantibody, a diabody, and humanized variants of all of the above, all ofwhich are within the skill in the art).

[0075] The antibody or variant thereof is preferably useful in detectingor diagnosing the presence of HIV gp120 envelope protein, and thus HIV,in an animal. The antibody is also preferably prevents or attenuatesinfection of an animal exposed to HIV, to whom an effective quantity ofthe antibody or a variant thereof, has been administered or produced inresponse to inoculation with the immunizing compound. The antibodypreferably also is useful in treating or preventing (i.e., inhibiting)HIV infection in an animal to whom a suitable dose has been administeredor in which a suitable quantity of antibody has been produced. Theantibody is also useful in the study of XIV infection of mammaliancells, the host range specificities of HIV infection, and preferably,the mechanism by which antibodies neutralize infectious viruses.

EXAMPLES

[0076] The following examples further illustrate the present inventionbut, of course, should not be construed as limiting the scope of theclaimed invention in any way.

[0077] Synthetic peptide arrays were constructed in 96-well microtiterplates in accordance with the method set forth in WO 91/02714(Saxinger), and used to test the binding of HIV-1_(LAI) envelope gp120that had been labeled with radioactive iodine (radiolabeling by standardmethods). After incubating the radiolabeled gp120 in a well with eachsynthetic peptide, a washing step was performed to remove unbound label,and the relative level of radioactivity remaining in each well of theplate was evaluated to determine the relative affinity of each peptidefor the gp120. The synthesis of the peptides and the quantity of bindingbetween the synthetic peptides and the gp120 were found to be suitablyreproducible, precise, and sensitive. Initial screening of the entireprimary sequence of the chemokine and CD4 receptor molecules was taken18 amino acid residues at a time.

[0078] The authenticity of the binding signals generated by thistechnique has been repeatedly demonstrated by showing that antibodies toCCR5 and CXCR4 are able to inhibit the binding of radiolabeled gp120 tothe polypeptides derived from CCR5 and CXCR4 that show a high affinityfor binding with gp120. Additionally, the accuracy of the binding assayused hereinbelow is demonstrated by Example 7.

Example 1

[0079] This example identifies segments of the CCR5 co-receptor thatbind with gp120.

[0080] The first column in the table below indicates the number of theamino acid in the wild-type CCR5 receptor. The second column explicitlyidentifies the peptide sequence. The third column indicatesthe-radioactive counts recorded in twenty minutes (i.e., the cpm×20)after the background or non-specific counts had been subtracted. Thefourth column contains an X in each row for which the listed polypeptidebound with high affinity to gp120. The fifth and final column containsan X in each row wherein the listed sequence binds with substantialaffinity but is weak in comparison to other samples, particularlyadjacent samples. Counts per 20′ Average- SEQ back- Peak non-Peak SEGPEPTIDE ground Activity activity empty (control) 7 1--18MDYQVSSPIYDINYYTSE 735 X 5--22 VSSPIYDINYYTSEPCQK 383 X 9--26IYDINYYTSEPCQKINVK 228 X 13-30 NYYTSEPCQKINVKQIAA 6 17-34SEPCQKINVKQIAARLLP −44 21-38 QKINVKQIAARLLPPLYS 20 25-42VKQIAARLLPPLYSLVFI 18 29-46 AARLLPPLYSLVFIFGFV 33 33-50LPPLYSLVFIFGFVGNML 705 X 37-54 YSLVFIFGFVGNMlVILI 347 X 41-58FIFGFVGNMLVILILINC 343 X 45-62 FVGNMLVILILINCKRLK 62 49-66MLVILILINCKRLKSMTD 84 53-70 LILINCKRLKSMTDIYLL 2 57-74NCKRLKSMTDIYLLNLAI 25 61-78 LKSMTDIYLLNLAISDLF 210 65-82TDIYLLNLAISDLFFLLT 38 69-86 LLNLAISDLFFLLTVPFW 144 73-90AISDLFFLLTVPFWAHYA 41 77-94 LFFLLTVPFWAHYAAAQW 173 81-98LTVPFWAHYAAAQWDFGN 306 85- FWAHYAAAQWDFGNTMCQ 212 89- YAAAQWDFGNTMCQLLTG494 X 93- QWDFGNTMCQLLTGLYFI 1019 X 97- GNTMCQLLTGLYFIGFFS 941 X 101-CQLLTGLYFIGFFSGIFF 489 X 105- TGLYFIGFFSGIFFIILL 80 109-FIGFFSGIFFIILLTIDR 76 113- FSGIFFIILLTIDRYLAV 83 117- FFIILLTIDRYLAVVHAV77 121- LLTIDRYLAVVHAVFALK 31 125- DRYLAVVHAVFALKARTV 62 129-AVVHAVFALKARTVTFGV 34 133- AVFALKARTVTFGVVTSV 63 137- LKARTVTFGVWDSVITWV74 141- TVTFGVVTSVITWVVAVF −25 145- GVVTSVITWVVAVFASLP 69 149-SVITWVVAVFASLPGIIF 46 153- WVVAVFASLPGIIFTRSQ 87 157- VFASLPGIIFTRSQKEGL54 161- LPGIIFTRSQKEGLHYTC 118 165- IFTRSQKEGLHYTCSSHF 98 169-SQKEGLHYTCSSHFPYSQ 304 X 173- GLHYTCSSEFPYSQYQFW 301 X 177-TCSSHFPYSQYQFWKNFQ 367 X 181- HFPYSQYQFWKNFQTLKI 1008 X 185-SQYQFWKNFQTLKIVILG 1572 X 189- FWKNFQTLKIVILGLVLP 40 193-FQTLKIVILGLVLPLLVM 45 197- KIVILGLVLPLLVMVICY 65 201- LGLVLPLLVMVICYSGIL180 205- LPLLVMVICYSGILKTLL 68 209- VMVICYSGILKTLLRCRN −8 213-CYSGILKTLLRCRNEKKR 70 217- ILKTLLRCRNEKKRHRAV 19 221- LLRCRNEKKRHRAVRLIF102 225- RNEKKRHRAVRLIFTIMI 23 229- KRHRAVRLIFTIMIVYFL 36 233-AVRLIFTIMTVYFLFWAP 62 237- IFTIMIVYFLFWAPYNIV 121 241-MIVYFLFWAPYNIVLLLN 214 245- FLFWAPYNIVLLLNTFQE 616 X 249-APYNIVLLLNTFQEFFGL 1962 X 253- IVLLLNTFQEFFGLNNCS 2134 X 257-LNTFQEFFGLNNCSSSNR 293 X 261- QEFFGLNNCSSSNRLDQA 63 265-GLNNCSSSNRLDQAMQVT −31 269- CSSSNRLDQAMQVTETLG 90 273-NRLDQAMQVTETLGMTHC 10 277- QAMQVTETLGMTHCCINP 81 281- VTETLGMTHCCINPIIYA15 285- LGMTHCCINPIIYAFVGE 282 X 289- HCCINPIIYAFVGEKFRN 200 X 293-NPIIYAFVGEKFRNYLLV 162 X 297- YAFVGEKFRNYLLVFFQK 596 X 301-GEKFRNYLLVFFQKHIAK 69 305- RNYLLVFFQKHIAKRFCK 65 309- LVFFQKHIAKRFCKCCSI76 313- QKHIAKRFCKCCSIFQQE 23 317- AKRFCKCCSIFQQEAPER 64 321-CKCCSIFQQEAPERASSV 53 325- SIFQQEAPERASSVYTRS 100 329-QEAPERASSVYTRSTGEQ 84 333- ERASSVYTRSTGEQEISV 84 337- SVYTRSTGEQEISVGL47

[0081] These data indicate that, in addition to polypeptide sequencesderived from positions 1-18 of the CCR5 receptor, the polypeptidesequences LPPLYSLVFIFGFVGNML, QWDFGNTMCQLLTGLYFIGFFS,SQYQFWKNFQTLKIVILG, APYNIVLLLNTFQEFFGLNNCS, and YAFVGEKFRNYLLVFFQKcomprise multiple subsequences, each which is capable of binding toHIV-1 envelope gp120.

Example 2

[0082] This example identifies segments of the CXCR4 co-receptor thatbind with gp120.

[0083] The first column in the table below indicates the number of theamino acid in the wild-type CXCR4 receptor. The second column explicitlyidentifies the peptide sequence. The third and fourth columns indicatethe radioactive counts recorded in twenty minutes (i.e., the cpm×20)after the background or non-specific counts had been subtracted. Thefifth column contains an X in each row for which the listed polypeptidebound with high affinity to gp120. The sixth and final column containsan X in each row wherein the listed sequence binds with substantialaffinity but is weak in comparison to other samples, particularlyadjacent samples. Major Activ- Minor ity Activity SEQ SEG PEPTIDE PeakPeak empty (control) 412 0 1-18 MEGISIYTSDNYTEEMGS 3003 2591 X 5--22SIYTSDNYTEEMGSGDYD 483 71 9--26 SDNYTEEMGSGDYDSMKE 455 43 13-30TEEMGSGDYDSMKEPCFR 453 41 17-34 GSGDYDSMKEPCFREENA 384 −28 21-38YDSMKEPCFREENANFNK 465 53 25-42 KEPCFREENANFNKIFLP 664 252 29-46FREENANFNKIFLPTIYS 463 51 33-50 NANFNKIFLPTIYSIIFL 585 173 37-54NKIFLPTIYSIIFLTGIV 550 138 41-58 LPTIYSIIFLTGIVGNGL 530 118 45-62YSIIFLTGIVGNGLVILV 535 123 49-66 FLTGIVGNGLVILVMGYQ 658 246 53-70IVGNGLVILVMGYQKKLR 650 238 57-74 GLVILVMGYQKKLRSMTD 569 157 61-78LVMGYQKKLRSMTDKYRL 517 105 65-82 YQKKLRSMTDKYRLHLSV 511 99 69-86LRSMTDKYRLHLSVADLL 572 160 73-90 TDKYRLHLSVADLLFVIT 504 92 77-94RLHLSVADLLFVITLPFW 548 136 81-98 SVADLLFVITLPFWAVDA 665 253 85-102LLFVITLPFWAVDAVANW 475 63 89-106 ITLPFWAVDAVANWYFGN 542 130 93-110FWAVDAVANWYFGNFLCK 478 66 97-114 DAVANWYFGNFLCKAVHV 524 112 101-118NWYFGNFLCKAVHVIYTV 508 96 105-122 GNFLCKAVHVIYTVNLYS 643 231 109-126CKAVHVIYTVNLYSSVLI 655 243 113-130 HVIYTVNLYSSVLILAFI 530 118 117-134TVNLYSSVLILAFISLDR 654 242 121-138 YSSVLILAFISLDRYLAI 569 157 125-142LILAFISLDRYLAIVHAT 519 107 129-146 FISLDRYLAIVHATNSQR 503 91 133-150DRYLAIVHATNSQRPRKL 580 168 137-154 AIVHATNSQRPRKLLAEK 485 73 141-158ATNSQRPRKLLAEKVVYV 490 78 145-162 QRPRKLLAEKVVYVGVWI 539 127 149-166KLLAEKVVYVGVWIPALL 501 89 153-170 EKVVYVGVWIPALLLTIP 559 147 157-174YVGVWIPALLLTIPDFIF 536 124 161-178 WIPALLLTIPDFIFANVS 594 182 165-182LLLTIPDFIFANVSEADD 1418 1006 X 169-186 IPDFIFANVSEADDRYIC 850 438 X173-190 IFANVSEADDRYICDRFY 679 267 177-194 VSEADDRYICDRFYPNDL 569 157181-198 DDRYICDRFYPNDLWVVV 537 125 185-202 ICDRFYPNDLWVVVFQFQ 718 306189-206 FYPNDLWVVVFQFQHIMV 828 416 X 193-210 DLWVVVFQFQHIMVGLIL 834 422X 197-214 VVFQFQHIMVGLILPGIV 1001 589 X 201-218 FQHIMVGLILPGIVILSC 582170 205-222 MVGLILPGIVILSCYCII 579 167 209-226 ILPGIVILSCYCIIISKL 604192 213-230 IVILSCYCIIISKLSHSK 689 277 217-234 SCYCIIISKLSHSKGHQK 671259 221-238 IIISKLSHSKGHQKRKAL 569 157 225-242 KLSHSKGHQKRKALKTTV 542130 229-246 SKGHQKRKALKTTVILIL 552 140 233-250 QKRKALKTTVILILAFFA 695283 237-254 ALKTTVILILAFFACWLP 673 261 241-258 TVILILAFFACWLPYYIG 735323 245-262 ILAFFACWLPYYIGISID 596 184 249-266 FACWLPYYIGISIDSFIL 614202 253-270 LPYYIGISIDSFILLEII 851 439 257-274 IGISIDSFILLEIIKQGC 1146734 X 261-278 IDSFILLEIIKQGCEFEN 3884 3472 X 265-282 ILLEIIKQGCEFENTVHK529 117 269-286 IIKQGCEFENTVEKWISI 518 106 273-290 GCEFENTVHKWISITEAL676 264 277-294 ENTVHKWISITEALAFFH 727 315 281-298 HKWISITEALAFFHCCLN575 163 285-302 SITEALAFFHCCLNPILY 600 188 289-306 ALAFFHCCLNPILYAFLG593 181 293-310 FHCCLNPILYAFLGAKFK 535 123 297-314 LNPILYAFLGAKFKTSAQ686 274 301-318 LYAFLGAKFKTSAQHALT 568 156 305-322 LGAKFKTSAQHALTSVSR612 200 309-326 FKTSAQHALTSVSRGSSL 585 173 313-330 AQNALTSVSRGSSLKILS559 147 317-334 LTSVSRGSSLKILSKGKR 595 183 321-338 SRGSSLKILSKGKRGGHS581 169 325-342 SLKILSKGKRGGHSSVST 697 285 329-346 LSKGKRGGHSSVSTESES597 185 333-350 KRGGHSSVSTESESSSFH 579 167 337-352 HSSVSTESESSSFHSS 515103

[0084] These data indicate that, in addition to polypeptide sequencesderived from positions 1-18 of the CXCR4 receptor, the polypeptidesequences LLLTIPDFIFANVSEADD (165-182), VVFQFQHIMVGLILPGIV (197-214),and IDSFILLEIIKQGCEFEN (261-278) comprise multiple subsequences, whichis capable of binding to HIV-1 envelope gp120.

Example 3

[0085] This example identifies segments of the STRL33 co-receptor thatbind with gp120.

[0086] The first column in the table below indicates the number of theamino acid in the wild-type STRL33 receptor. The second columnexplicitly identifies the peptide sequence. The third and fourth columnsindicate the radioactive counts recorded in twenty minutes (i.e., thecpm×20) after the background or non-specific counts had been subtracted.The fifth column contains an X in each row for which the listedpolypeptide bound with high affinity to gp120. The sixth and finalcolumn contains an X in each row wherein the listed sequence binds withsubstantial affinity but is weak in comparison to other samples,particularly adjacent samples. Ma- jor Ac- Minor tiv- Ac- ity tivity SEQSEG PEPTIDE Peak Peak empty (control) −34.5 34.5 1--18MAEHDYHEDYGFSSFNDS 1178.5 1320.5 X 5--22 DYHEDYGFSSFNDSSQEE 3357.53689.5 X 9--26 DYGFSSFNDSSQEEHQAF 8579.5 8909.5 X 13-30SSFNDSSQEEHQAFLQFS 2689.5 2757.5 X 17-34 DSSQEEHQAFLQFSKVFL 869.5 2152.5X 21-38 EEHQAFLQFSKVFLPCMY 2316.5 1819.5 X 25-42 AFLQFSKVFLPCMYLVVF1421.5 1359.5 X 29-46 FSKVFLPCMYLVVFVCGL 534.5 633.5 33-50FLPCMYLVVFVCGLVGNS 605.5 372.5 37-54 MYLVVFVCGLVGNSLVLV 168.5 235.541-58 VFVCGLVGNSLVLVISIF 570.5 284.5 45-62 GLVGNSLVLVISIFYHKL 164.5 95.549-66 NSIYLVISIFYHKLQSLT 1255.5 1378.5 X 53-70 LVISIFYHKLQSLTDVFL 1620.51780.5 X 57-74 IFYHKLQSLTDVFLVNLP 1275.5 1256.5 X 61-78KLQSLTDVFLVNLPLADL 412.5 348.5 65-82 LTDVFLVNLPLADLVFVC 233.5 336.569-86 FLVNLPLADLVFVCTLPF 70.5 51.5 73-90 LPLADLVFVCTLPFWAYA 557.5 960.5X 77-94 DLVFVCTLPFWAYAGIHE 1116.5 1063.5 X 81-98 VCTLPFWAYAGIHEWVFG1819.5 1754.5 X 85-102 PFWAYAGIHEWVFGQVMC 7262.5 7537.5 X 89-106YAGIHEWVFGQVMCKSLL 5911.5 6245.5 X 93-110 HEWVFGQVMCKSLLGIYT 3391.53466.5 X 97-114 FGQVMCKSLLGIYTINFY 1257.5 1354.5 X 101-118MCKSLLGIYTINFYTSML 1505.5 1283.5 105-122 LLGIYTINFYTSMLILTC 499.5 408.5109-126 YTINFYTSMLILTCITVD 351.5 510.5 113-130 FYTSMLILTCITVDRFIV 744.5907.5 117-134 MLILTCITVDRFIVVVKA 298.5 228.5 121-138 TCITVDRFIVVVKATKAY89.5 346.5 125-142 VDRFIVVVKATKAYNQQA 103.5 53.5 129-146IVVVKATKAYNQQAKRMT 166.5 43.5 133-150 KATKAYNQQAKRMTWGKV 701.5 568.5137-154 AYNQQAKRMTWGKVTSLL 55.5 4.5 141-158 QAKRMTWGKVTSLLIWVI −71.5−31.5 145-162 MTWGKVTSLLIWVISLLV −0.5 −26.5 149-166 KVTSLLIWVISLLVSLPQ−39.5 −118.5 153-170 LLIWVISLLVSLPQIIYG 42.5 75.5 157-174VISLLVSLPQIIYGNVFN −60.5 −127.5 161-178 LVSLPQIIYGNVFNLDKL 91.5 −15.5165-182 PQIIYGNVFNLDKLICGY −18.5 −37.5 169-186 YGNVFNLDKLICGYHDEA −41.5−20.5 173-190 FNLDKLICGYHDEAISTV 1072.5 1078.5 X 177-194KLICGYHDEAISTVVLAT 1363.5 1604.5 X 181-198 GYHDEAISTVVLATQMTL 754.51181.5 X 185-202 EAISTVVLATQMTLGFFL 3973.5 3745.5 X 189-206TVVLATQMTLGFFLPLLT 2327.5 2389.5 X 193-210 ATQMTLGFFLPLLTMIVC 2365.52444.5 X 197-214 TLGFFLPLLTMIVCYSVI 2387.5 479.5 201-218FLPLLTMIVCYSVIIKTL 1270.5 1195.5 X 205-222 LTMIVCYSVIIKTLLHAG 2787.52654.5 X 209-226 VCYSVIIKTLLHAGGFQK 1334.5 1143.5 X 213-230VIIKTLLHAGGFQKERSL 961.5 682.5 217-234 TLLHAGGFQKHRSLKIIF 1041.5 999.5221-238 AGGFQKHRSLKIIFLVMA 340.5 260.5 225-242 QKHRSLKIIFLVMAVFLL 810.5814.5 229-246 SLKIIFLVMAVFLLTQMP 612.5 853.5 233-250 IFLVMAVFLLTQMPFNLM386.5 772.5 237-254 MAVFLLTQMPFNLMKFIR 2263.5 2842.5 X 241-258LLTQMPFNLMKFIRSTHW 2513.5 3154.5 X 245-262 MPFNLMKFIRSTHWEYYA 2171.52182.5 X 249-266 LMKFIRSTHWEYYAMTSF 934.5 949.5 253-270IRSTHWEYYAMTSFHYTI 1571.5 1807.5 X 257-274 HWEYYAMTSFHYTIMVTE 2040.53065.5 X 261-278 YAMTSFHYTIMVTEAIAY 2688.5 2359.5 X 265-282SFHYTIMVTEAIAYLRAC 761.5 1033.5 269-286 TIMVTEAIAYLRACLNPV 140.5 272.5273-290 TEAIAYLRACLNPVLYAF 604.5 480.5 277-294 AYLRACLNPVLYAFVSLK 1802.51849.5 X 281-298 ACLNPVLYAFVSLKFRKN 4173.5 4515.5 X 285-302PVLYAFVSLKFRKNFWKL 1859.5 2147.5 X 289-306 AFVSLKFRKNFWKLVKDI 808.51040.5 293-310 LKFRKNFWKLVKDIGCLP 920.5 957.5 297-314 KNFWKLVKDIGCLPYLGV143.5 82.5 301-318 KLVKDIGCLPYLGVSHQW −2.5 27.5 305-322DIGCLPYLGVSHQWKSSE 17.5 78.5 309-326 LPYLGVSHQWKSSEDNSK 111.5 122.5313-330 GVSNQWKSSEDNSKTFSA 208.5 306.5 317-334 QWKSSEDNSKTFSASHNV 464.5533.5 321-338 SEDNSKTFSASHNVEATS 524.5 .434.5 325-342 SKTFSASHNVEATSMFQL1524.5 1239.5 X

[0087] These data indicate that, in addition to polypeptide sequencesderived from positions 9-26 of the STRL33 receptor, the polypeptidesequences LVISIFYHKLQSLTDVFL (53-70), PFWAYAGIHEWVFGQVMC (85-102),EAISTVVLATQMTLGFFL (185-202), LTMIVCYSVIIKTLLHAG (205-222),MAVFLLTQMPFNLMKFIRSTHW (237-342) comprise multiple subsequences, whichis capable of binding to HIV-1 envelope gp120.

Example 4

[0088] This example identifies segments of the human CD4 protein thatbind with gp120.

[0089] The second column in the in the table below identifies the aminoacid residue sequence of the polypeptide employed in the assay. Thefirst column identifies the sequence coordinates of human CD4 that havean identical amino acid sequence. The third column indicates the numberof radioactive decays (i.e., counts) that were counted, which isindicative of the affinity of the synthetic polypeptide for the gp120protein. In the table below, polypeptides retaining more than 4,000counts identify fragments that have a substantial capability to bindwith gp120. Polypeptides retaining more than 6,000 counts have moresubstantial binding affinity. Polypeptides retaining at least about10,000 counts have a substantial and strong capacity to bind to gp120.Of course, fragments corresponding to amino acid coordinates 101-121 and106-126 have a substantial, strong, and dominant capacity to bind togp120. B1 ( 1) 1-21 MNRGVPFRRLLLVLQLALLPA 3587 C1 ( 2) 16-26PFRELLLVLQLALLPAATQGK 4356 D1 ( 3) 11-31 LLVLQLALLPAATQGKKVVLG 1785 E1 (4) 16-36 LALLPAATQGKKVVLGKKGDT 1759 F1 ( 5) 21-41 AATQGKKVVLGKKGDTVELTC1562 G1 ( 6) 26-46 KKVVLGKKGDTVELTCTASQK 1910 H1 ( 7) 31-51GKKGDTVELTCTASQKKSIQF 1831 A2 ( 8) 36-56 TVELTCTASQKKSIQFHWKNS 1732 B2 (9) 41-61 CTASQKKSIQFHWKNSNQIKI 1717 C2 (10) 46-66 KKSIQFHWKNSNQIKILGNQG2182 D2 (11) 51-71 FHWKNSNQIKILGNQGSFLTK 1835 E2 (12) 56-76SNQIKILGNQGSFLTKGPSKL 1487 F2 (13) 61-81 ILGNQGSFLTKGPSKLNDRAD 1467 G2(14) 66-86 GSFLTKGPSKLNDRADSRRSL 1844 H2 (15) 71-91KGPSKLNDRADSRRSLWDQGN 1912 A3 (16) 76-96 LNDRADSRRSLWDQGNFPLII 1753 B3(17) 81-101 DSRRSLWDQGNFPLIIKNLKI 2224 C3 (18) 86-106LWDQGNFPLIIKNLKIEDSDT 3264 D3 (19) 91-111 NFPLIIKNLKIEDSDTYICEV 11646 E3(20) 96-116 IKNLKIEDSDTYICEVEDQKE 8439 F3 (21) 101-121IEDSDTYICEVEDQKEEVQLL 6803 G3 (22) 106-126 TYICEVEDQKEEVQLLVFGLT 44965H3 (23) 111-131 VEDQKEEVQLLVFGLTANSDT 36249 A4 (24) 116-136EEVQLLVFGLTANSDTHLLQG 14171 B4 (25) 121-141 LVFGLTANSDTHLLQGQSLTL 3683C4 (26) 126-146 TANSDTHLLQGQSLTLTLESP 6114 D4 (27) 131-151THLLQGQSLTLTLESPPGSSP 2552 E4 (28) 136-156 GQSLTLTLESPPGSSPSVQCR 1538 F4(29) 141-161 LTLESPPGSSPSVQCRSPRGK 1476 G4 (30) 146-166PPGSSPSVQCRSPRGKNIQGG 1496 H4 (31) 151-171 PSVQCRSPRGKNIQGGKTLSV 1400 A5(32) 156-176 RSPRGKNIQGGKTLSVSQLEL 2066 B5 (33) 161-181KNIQGGKTLSVSQLELQDSGT 3078 C5 (34) 166-186 GKTLSVSQLELQDSGTWTCTV 2618 D5(35) 171-191 VSQLELQDSGTWTCTVLQNQK 3879 E5 (36) 176-196LQDSGTWTCTVLQNQKKVEFK 2456 F5 (37) 181-201 TWTCTVLQNQKKVEFKIDIVV 4030 G5(38) 186-206 VLQNQKKVEFKIDIVVLAFQK 9737 H5 (39) 191-211KKVEFKIDIVVLAFQKASSIV 6313 A6 (40) 196-216 KIDIVVLAFQKASSIVYKKEG 3681 B6(41) 201-221 VLAFQKASSIVYKKEGEQVEF 3566 C6 (42) 206-226KASSIVYKKEGEQVEFSFPLA 14347 D6 (43) 211-231 VYKKEGEQVEFSFPLAFTVEK 14740E6 (44) 216-236 GEQVEFSFPLAFTVEKLTGSG 18549 F6 (45) 221-241FSFPLAFTVEKLTGSGELWWQ 9673 G6 (46) 226-246 AFTVEKLTGSGELWWQAERAS 3992 H6(47) 231-251 KLTGSGELWWQAERASSSKSW 1878 A7 (48) 236-256GELWWQAERASSSKSWITFDL 2730 B7 (49) 241-261 QAERASSSKSWITFDLINKEV 2588 C7(50) 246-266 SSSKSWITFDLKNKEVSVKRV 1761 D7 (51) 251-271WITFDLKNKEVSVKRVTQDPK 2126 E7 (52) 256-276 LKNKEVSVKPVTQDPKLQMGK 2288 F7(53) 261-281 VSVKRVTQDPKLQMGKKLPLH 1848 G7 (54) 266-286VTQDPKLQMGKKLPLHLTLPQ 2075 H7 (55) 271-291 KLQMGKKLPLHLTLPQALPQY 1949 A8(56) 276-296 KKLPLHLTLPQALPQYAGSGN 1922 B8 (57) 281-301HLTLPQALPQYAGSGNLTLAL 2394 C8 (58) 286-306 QALPQYAGSGNLTLALEAKTG 2364 D8(59) 291-311 YAGSGNLTLALEAKTGKLHQE 1830 E8 (60) 296-316NLTLALEAKTGKLHQEVNLVV 1676 F8 (61) 301-321 LEAKTGKLHQEVNLVVMRATQ 1729 G8(62) 306-326 GKLHQEVNLVVMRATQLQKNL 1776 ES (63) 311-331EVNLVVMRATQLQKNLTCEVW 2183 A9 (64) 316-336 VMRATQLQKNLTCEVWGPTSP 2144 B9(65) 321-341 QLQKNLTCEVWGPTSPKLMLS 1856 C9 (66) 326-346LTCEVWGPTSPKLMLSLKLEN 2412 D9 (67) 331-351 WGPTSPKLMLSLKLENKEAKV 2414 E9(68) 336-356 PKLMLSLKLENKEAKVSKREK 1656 F9 (69) 341-361SLKLENKEAKVSKREKAVWVL 1663 G9 (70) 346-366 NKEAKVSKREKAVWVLNPEAG 1735 H9(71) 351-371 VSKREKAVWVLNPEAGMWQCL 2034 A10 (72) 356-376KAVWVLNPEAGMWQCLLSDSG 3133 B10 (73) 361-381 LNPEAGMWQCLLSDSGQVLLE 6316C10 (74) 366-386 GMWQCLLSDSGQVLLESNIKV 4185 D10 (75) 371-391LLSDSGQVLLESNIKVLPTWS 2375 E10 (76) 376-396 GQVLLESNIKVLPTWSTPVQP 2089F10 (77) 381-401 ESNIKVLPTWSTPVQPMALIV 1992 G10 (78) 386-406VLPTWSTPVQPMALIVLGGVA 2197 E10 (79) 391-411 STPVQPMALIVLGGVAGLLLF 2527A11 (80) 396-416 PMALIVLGGVAGLLLFIGLGI 3067 B11 (81) 401-421VLGGVAGLLLFIGLGIFFCVR 3738 C11 (82) 406-426 AGLLLFIGLGIFFCVRCRHRR 2099D11 (83) 411-431 FIGLGIFFCVRCRHRRRQAER 1900 E11 (84) 416-436IFFCVRCRHRRRQAERMSQIK 2085 F11 (85) 421-441 RCRHRRRQAERMSQIKRLLSE 2075G11 (86) 42E-446 RRQAERMSQLKRLLSEKKTCQ 1607 H11 (87) 431-451RMSQIKRLLSEKKTCQCPHRF 2020 A12 (88) 436-456 KRLLSEKKTCQCPERFQKTCS 1674B12 (89) 441-458 EKKTCQCPHRFQKTCSPI 2006 A1 ( 0) empty (control) 2075

Example 5

[0090] This example shows the binding of ¹²⁵I-HIV-1_(LAI) gp120 to theamino termini of CCR5, CXCR4, and STRL33 as a function of the dependenceon position and length. Synthetic peptide arrays of nonapeptides,dodecapeptides, pentadecapeptides and octadecapeptides derived from CCR5(panel A), CXCR4 (panel B) and STRL33 (panel C) amino terminal domainswere prepared and utilized to test the binding of ¹²⁵I-HIV-1_(LAI)envelope gp120. Ordinal sequence position numbers are given inaccordance with the sequence data provided by the Genbank database forCCR5 (accession No. g1457946, gi|1457946), CXCR4 (accession No. g539677,gi|400654, sp|P30991) and STRL33 (accession No. g2209288, gi|2209288).The counts shown are the counts detected in each well minus thebackground counts (i.e., counts observed in the assay when nopolypeptide was bound to the well of the 96-well assay plate). PeptideSequence Panel A Scanning Windows (In Binding Results CCR5 each sequencerow 9-, For Window Length Initial 12-, 15-, isomers (counts bound-Sequence share the same initial background # starting point.) (nopeptide)) XXXXXXXXX      9 9 XXXXXXXXXXXX    12 12 XXXXXXXXXXXXXXX   1515 XXXXXXXXXXXXXXXXXX  18 18 1 MDYQVSSPIYDINYYTSE 543 2682 4976 5880 2DYQVSSPIYDINYYTSEP 1552 3089 5401 6363 3 YQVSSPIYDINYYTSEPC 2533 53055415 6119 4 QVSSPIYDINYYTSEPCQ 490 1959 4594 5645 5 VSSPIYDINYYTSEPCQK509 1629 3280 3521 6 SSPIYDINYYTSEPCQKI 671 1739 3498 3285 7SPIYDINYYTSEPCQKIN 1503 3463 4575 3234 8 PIYDINYYTSEPCQKINV 1186 22852682 2036 9 IYDINYYTSEPCQKTNVK 1359 2702 2516 1261 10 YDINYYTSEPCQKINVKQ4379 5245 3052 1913 11 DINYYTSEPCQKINVKQI 1396 1361 1144 712 12INYYTSEPCQKINVKQIA 1384 1190 707 684 13 NYYTSEPGQKINVKQIAA 1548 977 760595 14 YYTSEPCQKINVKQIAAR 1029 1052 847 638 15 YTSEPCQKINVKQIA 567 507459 16 TSEPCQKINVKQIAA 440 427 509 17 SEPCQKINVKQIAAR 434 430 426 18BPCQKINVKQIA 397 432 19 PCQKINVKQIAA 386 385 20 CQKINVKQIAAR 435 581 21QKINVKQIA 453 22 KINVKQIAA 487 23 INVKQIAAR 474

[0091] Panel B Peptide Sequence Binding Results CXCR4 Scanning WindowsFor Window Initial (In each sequence row 9-, 12-, 15-, 18- Length(counts Sequence # mers share the same initial starting point.)bound-background) XXXXXXXXX      9 9 XXXXXXXXXXXX    12 12XXXXXXXXXXXXXXX   15 15 XXXXXXXXXXXXXXXXXX  18 18 1 MEGISIYTSDNYTEEMGS591 334 3275 2079 2 EGISJYTSDNYTEEMGSG ^(a) 886 7255 1548 3GISIYTSDNYTEEMGSGD 454 2644 3274 1217 4 ISIYTSDNYTEEMGSGDY 466 3973 2202861 5 SLYTSDNYTEEMGSGDYD ^(a) 288 168 239 6 IYTSDNYTEEMGSGDYDS 332 335195 173 7 YTSDNYTEEMGSGDYDSM 181 161 201 103 8 TSDNYTEEMGSGDYDSMK ^(a)54 119 38 9 SDNYTEEMGSODYDSMKE 151 149 124 161 10 DNYTEEMGSGDYDSMKEP 67121 57 102 11 NYTEEMGSGDYDSMKEPC ^(a) 100 30 134 12 YTEEMGSGDYDSMKEPCF68 213 70 103 13 TEEMGSGDYDSMKEPCFR 146 67 23 47 14 EEMGSGDYDSMKEPCFRB^(a) 61 121 130 15 EMGSGDYDSMKEPCFREE 64 36 69 64 16 MGSGDYDSMKEPCFREEN57 68 64 129 17 GSGDYDSMKEPCFREENA ^(a) 155 172 155 18SGDYDSMKEPCFREENAN 100 118 186 89 19 GDYDSMKEPCFREENANF 53 167 198 13420 DYDSMKEPCFREENANFN ^(a) 167 146 75 21 YDSMKEPCFREENANFNK 171 144 8089 22 DSMKEPCFREENANFNKI 85 144 146 40 23 SMKEPCFREENANFN ^(a) 119 55 24MKEPCFREBNANFNK 188 133 74 25 KEPCFREENANFNKI 165 105 93 26 EPCFREENANFN^(a) 69 27 PCFREENANFNK 104 108 28 CFREENANFNKI 103 66 29 REENANFNK 58

[0092] Peptide Sequence Panel C Scanning Windows STRL33 (In eachsequence row Binding Initial 9-, 12-, 15-, 18-mers Results For WindowSequence share the same initial Length (counts # starting point.)bound-background) XXXXXXXXX     9 9 XXXXXXXXXXXX   12 12XXXXXXXXXXXXXXX  15 15 XXXXXXXXXXXXXXXXXX 18 18 1 MAEHDYHEDYGFSSFNDS 160625 1239 1386 2 AEHDYHEDYGFSSFNDSS 354 697 1095 1014 3EHDYHEDYGFSSFNDSSQ 509 937 2235 1219 4 HDYHEDYGFSSFNDSSQE 708 1427 17721500 5 DYHEDYGFSSFNDSSQEE 851 1554 1240 1191 6 YHEDYGFSSFNDSSQEEH 7281950 1357 985 7 HEDYGFSSFNDSSQEEHQ 729 1077 947 537 8 EDYGFSSFNDSSQEEHQA953 817 1152 548 9 DYGFSSFNDSSQEEHQAF 701 573 595 440 10YGFSSFNDSSQEEHQAFL 345 745 645 1138 11 GFSSFNDSSQEEEQAFLQ 171 480 2701639 12 FSSFNDSSQEEHQAFLQF 249 403 361 3608 13 SSFNDSSQEEHQAFLQFS 243277 902 6038 14 SFWDSSQEEEQAFLQFSK 304 303 969 4537 15FNDSSQEEEQAFLQFSKV 246 470 4089 4678 16 NDSSQEEHQAFLQFS 180 497 6160 17DSSQEEHQAFLQFSK 147 882 4588 18 SSQEEEQAFLQFSKV 287 4455 4732 19SQEEHQAFLQFS 647 7512 20 QEEHQAFLQFSK 1109 5672 21 EEHQAFLQFSKV 60605598 22 EHQAFLQFS 7505 23 HQAFLQFSK 2761 24 QAFLQFSKV 2600

Example 6

[0093] This example shows ¹²⁵I-HIV-1_(LAI) gp120 binding to N-terminalpeptide variants of CCR5, CXCR4 and STRL33.

[0094] Octadecapeptide alanine replacement variants of maximum gp120binding activity peaks were synthesized and tested for ¹²⁵-HIV-1_(LAI)gp120 binding. Each binding value presented is the average of twoseparate synthesis and binding experiments. Relative percentage ofControl={[(mean counts/Control counts)]×100%}±average deviation.Background counts (no peptide, see Example 7) were subtracted from allvalues. Data for CCR5 are presented in Panel A; data for CXCR4 arepresented in Panel B; and data for STRL33 are presented in Panel C.Panel A. ¹²⁵I-HIV-1_(LAI) gp120 binding to N-terminal peptide variantsof CCR5 CCR5 variant peptides (1-18) Relative % of Control^(a) ControlMDYQVSSPIYDINYYTSE 100 M1A ADYQVSSPIYDINYYTSE 167 ± 4  D2AMAYQVSSPIYDINYYTSE 125 ± 8  Y3A MDAQVSSPIYDINYYTSE 51 ± 2 Q4AMDYAVSSPIYDINYYTSE 104 ± 7  V5A MDYQASSPIYDINYYTSE 82 ± 3 S6AMDYQVASPIYDINYYTSE 124 ± 3  S7A MDYQVSAPIYDINYYTSE 56 ± 2 P8AMDYQVSSAIYDINYYTSE 157 ± 2  19A MDYQVSSPAYDINYYTSE 24 ± 7 Y10AMDYQVSSPIADINYYTSE 19 ± 6 D11A MDYQVSSPIYAINYYTSE  63 ± 22 I12AMDYQVSSPIYDANYYTSE 14 ± 1 N13A MDYQVSSPIYDIAYYTSE 253 ± 19 Y14AMDYQVSSPIYDINAYTSE   15 ± 0.3 Y15A MDYQVSSPIYDINYATSE 21 ± 5 T16AMDYQVSSPIYDINYYASE  78 ± 34 S17A MDYQVSSPIYDINYYTAE 64 ± 6 E18AMDYQVSSPIYDINYYTSA  4 ± 2

[0095] Panel B ¹²⁵I-HIV-1_(LAI)gp120 binding to N-terminal peptidevariants of CXCR4 CXCR4 variant peptides (1-18) Relative % ofControl^(a) Control MEGISIYTSDNYTEEMGS 100 M1A AEGISIYTSDNYTEEMGS 118± 18 E2A MAGISIYTSDNYTEEMGS   36 ± 0.3 G3A MEAISIYTSDNYTEEMGS 101 ± 3 I4A MEGASIYTSDNYTEEMGS    6 ± 0.3 S5A MEGIAIYTSDNYTEEMGS 133 ± 5  I6AMEGISAYTSDNYTEEMGS  2 ± 1 Y7A MEGISIATSDNYTEEMGS    7 ± 0.4 T8AMEGISIYASDNYTEEDGS  97 ± 10 S9A MEGISIYTADNYTEEMGS 70 ± 4 D10AMEGISIYTSANYTEEMGS 71 ± 8 N11A MEGISIYTSDAYTEEMGS   38 ± 0.4 Y12AMEGISIYTSDNATEEMGS 28 ± 2 T13A MEGISIYTSDNYAEEMGS 70 ± 6 E14AMEGISIYTSDNYTAEMGS 72 ± 1 E15A MEGISIYTSDNYTEAMGS 56 ± 7 M16AMEGISIYTSDNYTEEAGS 88 ± 4 G17A MEGISIYTSDNYTEEMAS 68 ± 8 S18AMEGISIYTSDNYTEEMGA 79 ± 1

[0096] Panel C ¹²⁵I-HIV-1_(LAI)gp120 binding to N-terminal peptidevariants of STRL33 STRL33 variant peptides (21-38) Relative % ofControl^(a) Control EEHQAFLQFSKVFLPCMY 100 E21A AEHQAFLQFSKVFLPCMY 81± 2 E22A EAHQAFLQFSKVFLPCMY 70 ± 1 H23A EEAQAFLQFSKVFLPCMY 99 ± 1 Q24AEEHAAFLQFSKVFLPCMY 72 ± 1 A25A EEHQAFLQFSKVFLPCMY 101 ± 1  F26AEEHQAALQFSKVFLPCMY   32 ± 0.1 L27A EEHQAFAQFSKVFLPCMY 37 ± 2 Q28AEEEQAFLAFSKVFLPCMY   44 ± 0.4 F29A EEHQAFLQASKVFLPCMY 20 ± 1 S30AEEHQAFLQFAKVFLPCMY 92 ± 2 K31A EEHQAFLQFSAVFLPCMY 162 ± 2  V32AEEHQAFLQFSKAFLPCMY 51 ± 3 F33A EEHQAFLQFSKVALPCMY 45 ± 2 L34AEEHQAFLQFSKVFAPCMY 76 ± 1 P35A EEHQAFLQFSKVFLACMY 82 ± 3 C36AEEHQAFLQFSKVFLPAMY 53 ± 5 M37A EEHQAFLQFSKVFLPCAY 112 ± 4  Y38AEEHQAFLQFSKVFLPCMA 83 ± 2

Example 7

[0097] This example demonstrates that the binding of HIV-1 gp120envelope protein to the polypeptides of the present invention and to thechemokine receptors from which the present inventive polypeptides wereoriginally derived or inspired is conserved across the various speciesof HIV-1. This example also demonstrates that a step subsequent toinitial binding of gp120 to CCR5, CXCR4, STRL33, and CD4 is the mostlikely source of the phenomenon of host-range selectivity. Additionally,this example demonstrates that the underlying method is accurate in thatreceptor variants that are predicted to have an altered affinity forbinding with gp120, do in fact have a statistically similar alterationin affinity where comparable changes in the receptors have beenidentified in other work and the affinity for binding of gp120/effect oninfectivity has been measured.

[0098] This example examines the effect of particular mutations of CCR5that were studied in the work underlying the present invention and thatwere also studied by other artisans in the field.

[0099] The following table identifies a mutation in the first column.The first letter designates the wild-type amino acid present at theposition indicated by the number, and the letter A which terminates allentries in the first column indicates that the amino acid residuepresent in that position in the mutant polypeptide is alaninyl. Forexample, the first data row (i.e., the second row of the table) containsthe entry Y3A in the first column, which indicates that the tyrosineresidue at position 3 of the wild-type CCR5 is substituted by an alanineresidue.

[0100] The second column provides the percentage of binding exhibited bya mutant polypeptide compared to a wild-type polypeptide, when themethods used to elucidate the present invention are used in conjunctionwith radiolabeled HIV-1_(LAI) gp120 envelope protein. The third throughseventh columns provide similar data that have been extracted from thework of others in the field using a strain of HIV-1 virus indicated atthe top of each column. For example, row 2 of the following tableindicates that when the mutation Y3A is effected in the human CCR5chemokine receptor, then the resulting CCR5 polypeptide has 51.4% of theability to bind HIV-1_(LAI) gp120 envelope protein in comparison to anequivalent wild-type peptide. Similarly, HIV-1_(LAI) binds to the mutantpolypeptide with 79% of the affinity of a non-mutated CCR5 chemokinereceptor. gp120 YU2 ADA JF-RL 89.6 DH123 Y3A 51.4 n/a 79 82 n/a 42 Q4A104 85 132 111 67 105 Y10A 19.2 2 50 26 10 3 D11A 62.8 2 27 22 6 3 Y14A14.6 12 47 25 6 0 Y15A 21 30 3 3 1 0 E18A 4.1 45 12 12 3 10

[0101] Statistical analysis of these data indicates that the similaritybetween the binding affinity of each mutant peptide for gp120 elucidatedin this study is not more than about 25% likely to be causally unrelatedto the effects observed for YU2, and not more than about 4% likely to becausally unrelated to the effects observed for each of the other viruseslisted in the table above.

[0102] Additionally, the affinity measurements generated by theunderlying technique has been demonstrated to be accurate by(repetitively) showing that antibodies that specifically bind toradiolabeled gp120 are capable of preventing the binding of gp120 topolypeptides that have shown high affinity for binding with gp120 in theexperiments upon which the present invention is predicated. Thus, thisexample shows that the binding with chemokine receptors HIV-1 can beinhibited by the present inventive polypeptides, irrespective of thestrain of HIV-1 from which the gp120 protein is obtained.

Example 8

[0103] This example provides a characterization of the critical aminoacids in the amino-terminal segments of CCR5, CXCR4, and STRL33 that areessential for the ability of these polypeptides to bind with gp120.

[0104] In this example, the effect on binding that occurs to duesuccessive replacement of each amino acid with alanine is indicated,wherein a (+) signifies a decrease in binding affinity and a (>)signifies an enhancement in binding affinity. As is clear frominspection, the sequences are shown with that amino-terminus at top andthe carboxyl-terminus at bottom. CCR5 (1-18) CXCR4 (1-18) STRL33 (21-38)M> M E D E+ E Y++ G H Q I+++++ Q V S> A S I++++++ F+++ S+ Y+++++ L++ P>T Q+ I+++ S+ F+++ Y+++ D+ S D+ N++ K> I++++ Y++ V+ N> T F+ Y++++ E LY+++ E++ P T M C+ S+ G M E+++++ S Y

Example 9

[0105] This example employs the same technique as Example 4 and providesinformation similar to that available from Example 4.

[0106] The data below compares the ability of synthetic fragments of CD4to bind to labeled gp120. 9-mer, 12-mer, 15-mer, 18-mer, and 21-merswere selected based on the data from Examples 4. The relative bindingaffinities of each group of polypeptides can be determined by inspectionof the number of counts of radiolabeled gp120 that were retained by eachN-mer. Data supporting these conclusions are provided by Examples 10 and11. Peptide Gp120 starting Bound position # Active Peptides (counts)ACTIVE 9-MERS 105 DTYICEVED 1043 115 KEEVQLLVF 1273 116 EEVQLLVFG 3170117 EVQLLVFGL 2146 217 EQVEFSFPL 1032 218 QVEFSFPLLA 1205 219 VEFSFPLAF1064 ACTIVE 15-MERS 109 CEVEDQKEEVQLLVF 1729 110 EVEDQKEEVQLLVFG 2805111 VEDQKEEVQLLVFGL 3816 112 EDQKEEVQLLVFGLT 3633 113 DQKEEVQLLVFGLTA3905 114 QKEEVQLLVFGLTAN 3770 115 KEEVQLLVFGLTANS 3485 116EEVQLLVFGLTANSD 6423 117 EVQLLVFGLTANSDT 2689 130 DTHLLQGQSLTLTLE 1622131 THLLQGQSLTLTLES 1874 132 HLLQGQSLTLTLESP 1277 213 KKEGEQVEFSFPLAF1921 214 KEGEQVEFSFPLAFT 3253 215 EGEQVEFSFPLAFTV 3270 216GEQVEFSFPLAFTVE 4656 217 EQVEFSFPLAFTVEK 4135 218 QVEFSFPLAFTVEKL 2047ACTIVE 21-MERS 90 GNFPLIIKNLKIEDS 5248 DTYICE 91 NFPLIIKNLKIEDSD 7803TYICEV 92 FPLIIKNLKIEDSDT 13919 YICEVE 93 PLIIKNLKIEDSDTY 20145 ICEVED94 LIIKNLKIEDSDTYI 17108 CEVEDQ 95 IIKNLKIEDSDTYIC 11892 EVEDQK 96IKNLKIEDSDTYICE 15073 VEDQKE 97 KNLKIEDSDTYICEV 8789 EDQKEE 99LKIEDSDTYICEVED 5519 QKEEVQ 100 KIEDSDTYICEVEDQ 6325 KEEVQL 101IEDSDTYICEVEDQK 12064 EEVQLL 102 EDSDTYICEVEDQKE 4933 EVQLLV 103DSDTYICEVEDQKEE 30277 VQLLVF 104 SDTYICEVEDQKEEV 30319 QLLVFG 105DTYICEVEDQKEEVQ 25424 LLVFGL 106 TYICEVEDQKEEVQL 20191 LVFGLT 107YICEVEDQKEEVQLL 22884 VFGLTA 108 ICEVEDQKEEVQLLV 7276 FGLTAN 109CEVEDQKEEVQLLVF 3517 GLTANS 123 FGLTANSDTHLLQGQ 11529 SLTLTL 124GLTANSDTHLLQGQS 14065 LTLTLE 125 LTANSDTHLLQGQSL 17113 TLTLES 126TANSDTHLLQGQSLT 23595 LTLESP 204 FQKASSIVYKKEGEQ 9382 VEFSFP 205QKASSIVYKKEGEQV 24959 EFSFPL 206 KASSIVYKKEGEQVE 30873 FSFPLA 207ASSIVYKKEGEQVEF 25146 SFPLAF 208 SSIVYKKEGEQVEFS 28068 FPLAFT 209SIVYKKEGEQVEFSF 8165 PLAFTV 210 IVYKKEGEQVEFSFP 15620 LAFTVE 221FSFPLAFTVEKLTGS 4163 GELWWQ 222 SFPLAFTVEKLTGSG 2284 ELWWQA 223FPLAFTVEKLTGSGE 6276 LWWQAE 224 PLAFTVEKLTGSGEL 2647 WWQAER 225LAFTVEKLTGSGELW 3577 WQAERA ACTIVE 12-MERS 101 IEDSDTYICEVE 1107 112EDQKEEVQLLVF 1379 113 DQKEEVQLLVFG 1624 114 QKEEVQLLVFGL 1785 115KEEVQLLVFGLT 1774 116 EEVQLLVFGLTA 3261 117 EVQLLVFGLTAN 1838 133LLQGQSLTLTLE 1320 215 EGEQVEFSFPLA 1456 216 GEQVEFSFPLAF 1729 217EQVEFSFPLAFT 1556 218 QVEFSFPLAFTV 1636 ACTIVE 18-MERS 105 DTYICEVEDQKEE1648 VQLLV 106 TYICEVEDQKEEV 3794 QLLVF 107 YICEVEDQKEEVQ 4611 LLVFG 108ICEVEDQKEEVQL 3898 LVFGL 109 CEVEDQKEEVQLL 3797 VFGLT 110 EVEDQKEEVQLLV3647 FGLTA 111 VEDQKEEVQLLVF 3913 GLTAN 112 EDQKEEVQLLVFG 3416 LTANS 113DQKEEVQLLVFGL 3317 TANSD 114 QKEEVQLLVFGLT 3671 ANSDT 127 ANSDTHLLQGQSL1540 TLTLE 128 NSDTHLLQGQSLT 1726 LTLES 129 SDTHLLQGQSLTL 1260 TLESP 210IVYKKEGEQVEFS 5382 FPLAF 211 VYKKEGEQVEFSF 4307 PLAFT 212 YKKEGEQVEFSFP4839 LAFTV 213 KKEGEQVEFSFPL 4683 AFTVE 214 KEGEQVEFSFPLA 3117 FTVEK 215EGEQVEFSFPLAF 2164 TVEKL 216 GEQVEFSFPLAFT 1643 VEKLT

Example 10

[0107] This example provides data which enables those skilled in the artto arrive at the conclusions indicated in Examples 9 and 12. In thisexample, the counts of radiolabeled gp-120 retained by each peptideindicated in the left hand column are given in the right hand column.The first panel (panel A) provides data for 21-mers of CD4. Panel APEPTIDE COUNTS LWDQGNFPLIIKNLKIEDSDT 731 WDQGNFPLIIKNLKIEDSDTY 889DQGNFPLIIKNLKIEDSDTYI 1138 QGNFPLIIKNLKIEDSDTYIC 2242GNFPLIIKNLKIEDSDTYICE 5248 NFPLIIKNLKIEDSDTYICEV 7803FPLIIKNLKIEDSDTYICEVE 13919 PLIIKLNKIEDSDTYICEVED 20145LIIKNLKIEDSDTYICEVEDQ 17108 IIKNLKIEDSDTYICEVEDQK 11892IKNLKIEDSDTYICEVEDQKE 15073 KNLKIEDSDTYICEVEDQKEE 8789NLKIEDSDTYICEVEDQKEEV 2016 LKIEDSDTYICEVEDQKEEVQ 5519KIEDSDTYICEVEDQKEEVQL 6325 IEDSDTYICEVEDQKEEVQLL 12064EDSDTYICEVEDQKEEVQLLV 4933 DSDTYICEVEDQKEEVQLLVF 30277SDTYICEVEDQKEEVQLLVFG 30319 DTYICEVEDQKEEVQLLVFGL 25424TYICEVEDQKEEVQLLVFGLT 20191 YICEVEDQKEEVQLLVFGLTA 22884ICEVEDQKEEVQLLVFGLTAN 7276 CEVEDQKEEVQLLVFGLTANS 3517EVEDQKEEVQLLVFGLTANSD 1687 VEDQKEEVQLLVFGLTANSDT 646EDQKEEVQLLVFGLTANSDTH 562 DQKEEVQLLVFGLTANSDTHL 599QKEEVQLLVFGLTANSDTHLL 573 KEEVQLLVFGLTANSDTHLLQ 682EEVQLLVFGLTANSDTHLLQG 690 EVQLLVFGLTANSDTHLLQGQ 589VQLLVFGLTANSDTHLLQGQS 1099 QLLVFGLTANSDTHLLQGQSL 2057LLVFGLTANSDTHLLQGQSLT 860 LVFGLTANSDTHLLQGQSLTL 4677VFGLTANSDTHLLQGQSLTLT 2762 FGLTANSDTHLLQGQSLTLTL 11529GLTANSDTHLLQGQSLTLTLE 14065 LTANSDTHLLQGQSLTLTLES 17113TANSDTHLLQGQSLTLTLESP 23595 Empty (Control) 515 TWTCTVLQNQKKVEFKIDIVV1430 WTCTVLQNQKKVEFKIDIVVL 1616 TCTVLQNQKKVEFKIDIVVLA 1092CTVLQNQKKVEFKIDIVVLAF 2909 TVLQNQKKVEFKIDIVVLAFQ 3273VLQNQKKVEFKIDIVVLAFQK 1323 LQNQKKVEFKIDIVVLAFQKA 1256QNQKKVEFKIDIVVLAFQKAS 1808 NQKKVEFKIDIVVLAFQKASS 1507QKKVEFKIDIVVLAFQKASSI 759 KKVEFKIDIVVLAFQKASSIV 782KVEFKIDIVVLAFQKASSIVY 635 VEFKIDIVVLAFQKASSIVYK 725EFKIDIVVLAFQKASSIVYKK 649 FKIDIVVLAFQKASSIVYKKE 593KIDIVVLAFQKASSIVYKKEG 1394 IDIVVLAFQKASSIVYKKEGE 962DIVVLAFQKASSIVYKKEGEQ 788 IVVLAFQKASSIVYKKEGEQV 646VVLAFQKASSIVYKKEGEQVE 772 VLAFQKASSIVYKKEGEQVEF 1793LAFQKASSIVYKKEGEQVEFS 1410 AFQKASSIVYKKEGEQVEFSF 3775FQKASSIVYKKEGEQVEFSFP 9382 QKASSIVYKKEGEQVEFSFPL 24959KASSIVYKKEGEQVEFSFPLA 30873 ASSIVYKKEGEQVEFSFPLAF 25146SSIVYKKEGEQVEFSFPLAFT 28068 SIVYKKEGEQVEFSFPLAFTV 8165IVYKKEGEQVEFSFPLAFTVE 15620 VYKKEGEQVEFSFPLAFTVEK 2429YKKEGEQVEFSFPLAFTVEKL 735 KKEGEQVEFSFPLAFTVEKLT 1847KEGEQVEFSFPLAFTVEKLTG 972 EGEQVEFSFPLAFTVEKLTGS 739GEQVEFSFPLAFTVEKLTGSG 652 EQVEFSFPLAFTVEKLTGSGE 765QVEFSFPLAFTVEKLTGSGEL 741 VEFSFPLAFTVEKLTGSGELW 633EFSFPLAFTVEKLTGSGELWW 681 FSFPLAFTVEKLTGSGELWWQ 4163SFPLAFTVEKLTGSGELWWQA 2284 FPLAFTVEKLTGSGELWWQAE 6276PLAFTVEKLTGSGELWWQAER 2647 LAFTVEKLTGSGELWWQAERA 3577AFTVEKLTGSGELWWQAERAS 1739 Empty (control) 617

[0108] These second and third panels (panels B and C) provide data for 18-mers of a small region of CD4. Panel B PEPTIDE COUNTS LWDQGNFPLIIKNLK502 WDQGNFPLIIKNLKI 534 DQGNFPLIIKNLKIE 635 QGNFPLIIKNLKIED 509GNFPLIIKNLKIEDS 624 NFPLIIKNLKIEDSD 654 FPLIIKNLKIEDSDT 539PLIIKNLKIEDSDTY 661 LIIKNLKIEDSDTYI 542 IIKNLKIEDSDTYIC 664IKNLKIEDSDTYICE 568 KNLKIEDSDTYICEV 562 NLKIEDSDTYICEVE 1160LKIEDSDTYICEVED 846 KIEDSDTYICEVEDQ 1088 IEDSDTYICEVEDQK 1143EDSDTYICEVEDQKE 815 DSDTYICEVEDQKEE 973 SDTYICEVEDQKEEV 993DTYICEVEDQKEEVQ 1071 TYICEVEDQKEEVQL 956 YICEVEDQKEEVQLL 1064ICEVEDQKEEVQLLV 1084 CEVEDQKEEVQLLVF 1729 EVEDQKEEVQLLVFG 2805VEDQKEEVQLLVFGL 3816 EDQKEEVQLLVFGLT 3633 DQKEEVQLLVFGLTA 3905QKEEVQLLVFGLTAN 3770 KEEVQLLVFGLTANS 3485 EEVQLLVFGLTANSD 6423EVQLLVFGLTANSDT 2689 VQLLVFGLTANSDTH 1006 QLLVFGLTANSDTHL 865LLVFGLTANSDTHLL 599 LVFGLTANSDTHLLQ 609 VFGLTANSDTHLLQG 532FGLTANSDTHLLQGQ 625 GLTANSDTHLLQGQS 532 LTANSDTHLLQGQSL 634TANSDTHLLQGQSLT 513 ANSDTHLLQGQSLTL 542 NSDTHLLQGQSLTLT 631SDTHLLQGQSLTLTL 747 DTHLLQGQSLTLTLE 1622 THLLQGQSLTLTLES 1874HLLQGQSLTLTLESP 1277 LWDQGNFPLIIKNLKIED 582 WDQGNFPLIIKNLKIEDS 626DQGNFPLIIKNLKIEDSD 598 QGNFPLIIKNLKIEDSDT 564 GNFPLIIKNLKIEDSDTY 557NFPLIIKNLKIEDSDTYI 627 FPLIIKNLKIEDSDTYIC 509 PLIIKNLKIEDSDTYICE 624LIIKNLKIEDSDTYICEV 634 IIKNLKIEDSDTYICEVE 751 IKNLKIEDSDTYICEVED 699KNLKIEDSDTYICEVEDQ 708 NLKIEDSDTYICEVEDOK 863 LKIEDSDTYICEVEDQKE 872KIEDSDTYICEVEDQKEE 858 IEDSDTYICEVEDQKEEV 1230 EDSDTYICEVEDQKEEVQ 788DSDTYICEVEDQKEEVQL 961 SDTYICEVEDQKEEVQLL 870 DTYICEVEDQKEEVQLLV 1648TYICEVEDQKEEVQLLVF 3794 YICEVEDQKEEVQLLVFG 4611 ICEVEDQKEEVQLLVFGL 3898CEVEDQKEEVQLLVFGLT 3797 EVEDQKEEVQLLVFGLTA 3647 VEDQKEEVQLLVFGLTAN 3913EDQKEEVQLLVFGLTANS 3416 DQKEEVQLLVFGLTANSD 3317 QKEEVQLLVFGLTANSDT 3671KEEVQLLVFGLTANSDTH 1271 EEVQLLVFGLTANSDTHL 783 EVQLLVFGLTANSDTHLL 667VQLLVFGLTANSDTHLLQ 673 QLLVFGLTANSDTHLLQG 574 LLVFGLTANSDTHLLQGQ 568LVFGLTANSDTHLLQGQS 564 VFGLTANSDTHLLQGQSL 531 FGLTANSDTHLLQGQSLT 591GLTANSDTHLLQGQSLTL 572 LTANSDTHLLQGQSLTLT 528 TANSDTHLLQGQSLTLTL 891ANSDTHLLQGQSLTLTLE 1540 NSDTHLLQGQSLTLTLES 1726 SDTHLLQGQSLTLTLESP 1260Empty (control) 575

[0109] Panel C PEPTIDE COUNTS WTCTVLQNQKKVEFK 566 TCTVLQNQKKVEFKI 510CTVLQNQKKVEFKID 608 TVLQNQKKVEFKIDI 587 VLQNQKKVEFKIDIV 605LQNQKKVEFKIDIVV 644 QNQKKVEFKIDIVVL 636 NQKKVEFKIDIVVLA 860QKKVEFKIDIVVLAF 1333 KKVEFKIDIVVLAFQ 951 KVEFKIDIVVLAFQK 1051VEFKIDIVVLAFQKA 1005 EFKIDIVVLAFQKAS 1188 FKIDIVVLAFQKASS 1001KIDIVVLAFQKASSI 956 IDIVVLAFQKASSIV 865 DIVVLAFQKASSIVY 776IVVLAFQKASSIVYK 783 VVLAFQKASSIVYKK 577 VLAFQKASSIVYKKE 634LAFQKASSIVYKKEG 593 AFQKASSIVYKKEGE 544 FQKASSIVYKKEGEQ 637QKASSIVYKKEGEQV 519 KASSIVYKKEGEQVE 563 ASSIVYKKEGEQVEF 589SSIVYKKEGEQVEFS 558 SIVYKKEGEQVEFSF 651 IVYKKEGEQVEFSFP 615VYKKEGEQVEFSFPL 714 YKKEGEQVEFSFPLA 687 KKEGEQVEFSFPLAF 1921KEGEQVEFSFPLAFT 3253 EGEQVEFSFPLAFTV 3270 GEQVEFSFPLAFTVE 4656EQVEFSFPLAFTVEK 4135 QVEFSFPLAFTVEKL 2047 VEFSFPLAFTVEKLT 899EFSFPLAFTVEKLTG 920 FSFPLAFTVEKLTGS 672 SFPLAFTVEKLTGSG 565FPLAFTVEKLTGSGE 556 PLAFTVEKLTGSGEL 612 LAFTVEKLTGSGELW 579AFTVEKLTGSGELWW 586 FTVEKLTGSGELWWQ 625 TVEKLTGSGELWWQA 550VEKLTGSGELWWQAE 735 EKLTGSGELWWQAER 683 WTCTVLQNQKKVEFKIDI 588TCTVLQNQKKVEFKIDIV 571 CTVLQNQKKVEFKIDIVV 553 TVLQNQKKVEFKIDIVVL 655VLQNQKKVEFKIDIVVLA 724 LQNQKKVEFKIDIVVLAF 938 QNQKKVEFKIDIVVLAFQ 917NQKKVEFKIDIVVLAFQK 889 QKKVEFKIDIVVLAFQKA 1013 KKVEFKIDIVVLAFQKAS 912KVEFKIDIVVLAFQKASS 1011 VEFKIDIVVLAFQKASSI 819 EFKIDIVVLAFQKASSIV 799FKIDIVVLAFQKASSIVY 843 KIDIVVLAFQKASSIVYK 779 IDIVVLAFQKASSIVYKK 711DIVVLAFQKASSIVYKKE 660 IVVLAFQKASSIVYKKEG 531 VVLAFQKASSIVYKKEGE 560VLAFQKASSIVYKKEGEQ 549 LAFQKASSIVYKKEGEQV 665 AFQKASSIVYKKEGEQVE 514FQKASSIVYKKEGEQVEF 528 QKASSIVYKKEGEQVEFS 602 KASSIVYKKEGEQVEFSF 536ASSIVYKKEGEQVEFSFP 701 SSIVYKKEGEQVEFSFPL 756 SIVYKKEGEQVEFSFPLA 771IVYKKEGEQVEFSFPLAF 5382 VYKKEGEQVEFSFPLAFT 4307 YKKEGEQVEFSFPLAFTV 4839KKEGEQVEFSFPLAFTVE 4683 KEGEQVEFSFPLAFTVEK 3117 EGEQVEFSFPLAFTVEKL 2164GEQVEFSFPLAFTVEKLT 1643 EQVEFSFPLAFTVEKLTG 798 QVEFSFPLAFTVEKLTGS 736VEFSFPLAFTVEKLTGSG 533 EFSFPLAFTVEKLTGSGE 668 FSFPLAFTVEKLTGSGEL 613SFPLAFTVEKLTGSGELW 656 FPLAFTVEKLTGSGELWW 586 PLAFTVEKLTGSGELWWQ 650LAFTVEKLTGSGELWWQA 866 AFTVEKLTGSGELWWQAE 788 FTVEKLTGSGELWWQAER 1143Empty (control) 556

[0110] The fourth and fifth panels (Panels D and E) provide data forselect 9-mers and 12-mers of CD4. Panel D PEPTIDE COUNTS DQGNFPLII 662QGNFPLIIK 508 GNFPLIIKN 600 NFPLIIKNL 561 FPLIIKNLK 601 PLIIKNLKI 697LIIKNLKIE 515 IIKNLKIED 658 IKNLKIEDS 557 KNLKIEDSD 612 NLKIEDSDT 512LKIEDSDTY 492 KIEDSDTYI 603 IEDSDTYIC 567 EDSDTYICE 650 DSDTYICEV 712SDTYICEVE 819 DTYICEVED 1043 TYICEVEDQ 805 YICEVEDQK 728 ICEVEDQKE 596CEVEDQKEE 555 EVEDQKEEV 587 VEDQKEEVQ 521 EDQKEEVQL 564 DQKEEVQLL 589QKEEVQLLV 636 KEEVQLLVF 1273 EEVQLLVFG 3170 EVQLLVFGL 2146 VQLLVFGLT 815QLLVFGLTA 822 LLVFGLTAN 576 LVFGLTANS 522 VFGLTANSD 549 FGLTANSDT 563GLTANSDTH 481 LTANSDTHL 596 TANSDTHLL 554 ANSDTHLLQ 642 NSDTHLLQG 561SDTHLLQGQ 526 DTHLLQGQS 578 THLLQGQSL 512 HLLQGQSLT 564 LLQGQSLTL 568LQGQSLTLT 501 QGQSLTLTL 594 GQSLTLTLE 777 DQGNFPLIIKNL 604 QGNFPLIIKNLK533 GNFPLIIKNLKI 547 NFPLIIKNLKIE 647 FPLIIKNLKIED 511 PLIIKNLKIEDS 565LIIKNLKIEDSD 619 IIKNLKIEDSDT 511 IKNLKIEDSDTY 574 KNLKIEDSDTYI 523NLKIEDSDTYIC 639 LKIEDSDTYICE 635 KIEDSDTYICEV 601 IEDSDTYICEVE 1107EDSDTYICEVED 956 DSDTYICEVEDQ 937 SDTYICEVEDQK 846 DTYICEVEDQKE 720TYICEVEDQKEE 818 YICEVEDQKEEV 734 ICEVEDQKEEVQ 585 CEVEDQKEEVQL 561EVEDQKEEVQLL 508 VEDQKEEVQLLV 657 EDQKEEVQLLVF 1379 DQKEEVQLLVFG 1624QKEEVQLLVFGL 1785 KEEVQLLVFGLT 1774 EEVQLLVFGLTA 3261 EVQLLVFGLTAN 1838VQLLVFGLTANS 747 QLLVFGLTANSD 721 LLVFGLTANSDT 533 LVFGLTANSDTH 586VFGLTANSDTHL 548 FGLTANSDTHLL 571 GLTANSDTHLLQ 574 LTANSDTHLLQG 534TANSDTHLLQGQ 549 ANSDTHLLQGQS 559 NSDTHLLQGQSL 585 SDTHLLQGQSLT 540DTHLLQGQSLTL 527 THLLQGQSLTLT 646 HLLQGQSLTLTL 701 LLQGQSLTLTLE 1320Empty (control) 581

[0111] Panel E PEPTIDE COUNTS TVLQNQKKV 534 VLQNQKKVE 556 LQNQKKVEF 565QNQKKVEFK 537 NQKKVEFKI 597 QKKVEFKID 575 KKVEFKIDI 501 KVEFKIDIV 555VEFKIDIVV 548 EFKIDIVVL 665 FKIDIVVLA 568 KIDIVVLAF 665 IDIVVLAFQ 691DIVVLAFQK 686 IVVLAFQKA 602 VVLAFQKAS 600 VLAFQKASS 466 LAFQKASSI 592AFQKASSIV 595 FQKASSIVY 568 QKASSIVYK 494 KASSIVYKK 498 ASSIVYKKE 600SSIVYKKEG 515 SIVYKKEGE 566 IVYKKEGEQ 534 VYKKEGEQV 490 YKKEGEQVE 518KKEGEQVEF 546 KEGEQVEFS 595 EGEQVEFSF 735 GEQVEFSFP 697 EQVEFSFPL 1032QVEFSFPLA 1205 VEFSFPLAF 1064 EFSFPLAFT 658 FSFPLAFTV 472 SFPLAFTVE 619FPLAFTVEK 569 PLAFTVEKL 597 LAFTVEKLT 501 AFTVEKLTG 517 FTVEKLTGS 574TVEKLTGSG 487 VEKLTGSGE 585 EKLTGSGEL 541 KLTGSGELW 491 LTGSGELWW 550TGSGELWWQ 507 VLQNQKKVEFKI 503 LQNQKKVEFKID 508 QNQKKVEFKIDI 559NQKKVEFKIDIV 532 QKKVEFKIDIVV 595 KKVEFKIDIVVL 597 KVEFKIDIVVLA 560VEFKIDIVVLAF 681 EFKIDIVVLAFQ 659 FKIDIVVLAFQK 736 KIDIVVLAFQKA 689IDIVVLAFQKAS 630 DIVVLAFQKASS 746 IVVLAFQKASSI 548 VVLAFQKASSIV 567VLAFQKASSIVY 548 LAFQKASSIVYK 465 AFQKASSIVYKK 597 FQKASSIVYKKE 577QKASSIVYKKEG 596 KASSIVYKKEGE 559 ASSIVYKKEGEQ 523 SSIVYKKEGEQV 615SIVYKKEGEQVE 543 IVYKKEGEQVEF 533 VYKKEGEQVEFS 584 YKKEGEQVEFSF 548KKEGEQVEFSFP 598 KEGEQVEFSFPL 710 EGEQVEFSFPLA 1456 GEQVEFSFPLAF 1729EQVEFSFPLAFT 1556 QVEFSFPLAFTV 1636 VEFSFPLAFTVE 518 EFSFPLAFTVEK 585FSFPLAFTVEKL 573 SFPLAFTVEKLT 528 FPLAFTVEKLTG 622 PLAFTVEKLTGS 528LAFTVEKLTGSG 608 AFTVEKLTGSGE 511 FTVEKLTGSGEL 530 TVEKLTGSGELW 573VEKLTGSGELWW 477 EKLTGSGELWWQ 543 Empty (control) 571

[0112] Panels F and G provide data on sequential alanine replacementsfor selected CD4 polypeptides. Panel F PEPTIDE COUNTS ZZZZZZDTYICEVED5844 ZZZZZZATYICEVED 5921 ZZZZZZDAYICEVED 6362 ZZZZZZDTAICEVED 1301ZZZZZZDTYACEVED 2583 ZZZZZZDTYIAEVED 4483 ZZZZZZDTYICAVED 3154ZZZZZZDTYICEAED 3432 ZZZZZZDTYICEVAD 3595 ZZZZZZDTYICEVEA 5942ZZZZZZDTYICEVED 4973 ZZZZZZDTYICEVED 4775 ZZZZZZATYICEVED 4962ZZZZZZDAYICEVED 4163 ZZZZZZDTAICEVED 1384 ZZZZZZDTYACEVED 3085ZZZZZZDTYIAEVED 5128 ZZZZZZDTYICAVED 2587 ZZZZZZDTYICEAED 2499ZZZZZZDTYICEVAD 2706 ZZZZZZDTYICEVEA 6345 ZZZZZZDTYICEVED 5564EEVQLLVFGLTANSD 18582 AEVQLLVFGLTANSD 16220 EAVQLLVFGLTANSD 14220EEAQLLVFGLTANSD 18124 EEVALLVFGLTANSD 10890 EEVQALVFGLTANSD 11258EEVQLAVFGLTANSD 11954 EEVQLLAFGLTANSD 13317 EEVQLLVAGLTANSD 9573EEVQLLVFALTANSD 19348 EEVQLLVFGATANSD 10408 EEVQLLVFGLAANSD 19973EEVQLLVFGLTTNSD 20100 EEVQLLVFGLTAASD 19390 EEVQLLVFGLTANAD 17684EEVQLLVFGLTANSA 18227 EEVQLLVFGLTANSD 19738 EEVQLLVFGLTANSD 21338AEVQLLVFGLTANSD 14590 EAVQLLVFGLTANSD 13213 EEAQLLVFGLTANSD 16296EEVALLVFGLTANSD 13415 EEVQALVFGLTANSD 12603 EEVQLAVFGLTANSD 13690EEVQLLAFGLTANSD 16286 EEVQLLVAGLTANSD 11480 EEVQLLVFALTANSD 18254EEVQLLVFGATANSD 19978 EEVQLLVFGLAANSD 18863 EEVQLLVFGLTTNSD 20021EEVQLLVFGLTAASD 19200 EEVQLLVFGLTANAD 17928 EEVQLLVFGLTANSA 22206EEVQLLVFGLTANSD 18721 THLLQGQSLTLTLES 7756 AHLLQGQSLTLTLES 8602TALLQGQSLTLTLES 6931 THALQGQSLTLTLES 7683 THLAQGQSLTLTLES 7701THLLAGQSLTLTLES 4578 THLLQAQSLTLTLES 8471 TELLQGASLTLTLES 4238THLLQGQALTLTLES 8659 THLLQGQSATLTLES 4430 THLLQGQSLALTLES 8158THLLQGQSLTATLES 4380 THLLQGQSLTLALES 11699 THLLQGQSLTLTAES 862THLLQGQSLTLTLAS 2596 THLLQGQSLTLTLEA 5849 THLLQGQSLTLTLES 6545THLLQGQSLTLTLES 4787 AHLLQGQSLTLTLES 5826 TALLQGQSLTLTLES 5012THALQGQSLTLTLES 5059 THLAQGQSLTLTLES 5120 THLLAGQSLTLTLES 2956THLLQAQSLTLTLES 6393 THLLQGASLTLTLES 1933 THLLQGQALTLTLES 5151THLLQGQSATLTLES 1391 THLLQGQSLALTLES 4749 THLLQGQSLTATLES 813THLLQGQSLTLALES 8147 THLLQGQSLTLTAES 797 THLLQGQSLTLTLAS 2193THLLQGQSLTLTLEA 7984 THLLQGQSLTLTLES 5947 Empty (control) 569

[0113] Panel G PEPTIDE COUNTS GEQVEFSFPLAFTVE 20691 AEQVEFSFPLAFTVE18546 GAQVEFSFPLAFTVE 17733 GEAVEFSFPLAFTVE 17500 GEQAEFSFPLAFTVE 14764GEQVAFSFPLAFTVE 16668 GEQVEASFPLAFTVE 6793 GEQVEFAFPLAFTVE 21681GEQVEFSAPLAFTVE 7767 GEQVEFSFALAFTVE 20480 GEQVEFSFPAAFTVE 10024GEQVEFSFPLTFTVE 17397 GEQVEFSFPLAATVE 10130 GEQVEFSFPLAFAVE 20627GEQVEFSFPLAFTAE 18797 GEQVEFSFPLAFTVA 18371 GEQVEFSFPLAFTVE 17662GEQVEFSFPLAFTVE 19190 AEQVEFSFPLAFTVE 18042 GAQVEFSFPLAFTVE 18079GEAVEFSFPLAFTVE 19756 GEQAEFSFPLAFTVE 13000 GEQVAFSFPLAFTVE 13930GEQVEASFPLAFTVE 6533 GEQVEFAFPLAFTVE 20072 GEQVEFSAPLAFTVE 7378GEQVEFSFALAFTVE 19480 GEQVEFSFPAAFTVE 10589 GEQVEFSFPLTFTVE 18318GEQVEFSFPLAATVE 9572 GEQVEFSFPLAFAVE 19516 GEQVEFSFPLAFTAE 16765GEQVEFSFPLAFTVA 18187 GEQVEFSFPLAFTVE 18219 ZZZZZZDTYICEVED 5017ZZZZZZDTYICEVEZ 5421 ZZZZZZDTYICEVZZ 2166 ZZZZZZDTYICEZZZ 922ZZZZZZDTYIZZZZZ 564 ZZZZZZZTYICEVED 3031 EEVQLLVFGLTANSD 23357EEVQLLVFGLTANSZ 15808 EEVQLLVFGLTANZZ 16496 EEVQLLVFGLTAZZZ 14097EEVQLLVFGLTZZZZ 16473 EEVQLLVFGLZZZZZ 10516 EEVQLLVFGZZZZZZ 10372EEVQLLVFZZZZZZZ 7333 EEVQLLVZZZZZZZZ 1098 ZEVQLLVFGLTANSD 16716ZZVQLLVFGLTANSD 5281 ZZZQLLVFGLTANSD 4310 ZZZZLLVFGLTANSD 1026ZZZZZLVFGLTANSD 664 ZZZZZZVFGLTANSD 779 ZZZZZZZFGLTANSD 760ZZZZZZZZGLTANSD 657 EEVQLLVFGLTANSD 18040 THLLQGQSLTLTLES 10850THLLQGQSLTLTLEZ 10269 THLLQGQSLTLTLZZ 4668 THLLQGQSLTLTZZZ 908THLLQGQSLTLZZZZ 844 THLLQGQSLTZZZZZ 475 THLLQGQSLZZZZZZ 548THLLQGQSZZZZZZZ 570 THLLQGQZZZZZZZZ 442 ZHLLQGQSLTLTLES 11445ZZLLQGQSLTLTLES 11631 ZZZLQGQSLTLTLES 7993 ZZZZQGQSLTLTLES 6887ZZZZZGQSLTLTLES 3305 ZZZZZZQSLTLTLES 4453 ZZZZZZZSLTLTLES 1086ZZZZZZZZLTLTLES 1201 THLLQGQSLTLTLES 9756 GEQVEFSFPLAFTVE 18856GEQVEFSFPLAFTVZ 16222 GEQVEFSFPLAFTZZ 12535 GEQVEFSFPLAFZZZ 11384GEQVEFSFPLAZZZZ 5846 GEQVEFSFPLZZZZZ 4749 GEQVEFSFPZZZZZZ 2208GEQVEFSFZZZZZZZ 3277 GEQVEFSZZZZZZZZ 742 ZEQVEFSFPLAFTVE 19736ZZQVEFSFPLAFTVE 18684 ZZZVEFSFPLAFTVE 12892 ZZZZEFSFPLAFTVE 12166ZZZZZFSFPLAFTVE 2134 ZZZZZZSFPLAFTVE 1454 ZZZZZZZFPLAFTVE 1391ZZZZZZZZPLAFTVE 1489 GEQVEFSFPLAFTVE 18867 empty (control) 580

Example 11

[0114] This example characterizes CD4 receptor sequences found to haveHIV gp120 binding activity in screening tests. Panel A displaysinformation obtained from sequential replacement of amino acid residuesby alaninyl residues. In panel A, a (+) signifies a decrease in bindingaffinity whereas a (>) indicates that replacement of the residue by analaninyl residue yields an increase in binding affinity. Sequences areshown with amino-terminus at the top and the carboxyl-terminus at thebottom. Right and left sides are from independent assays. Panel A.105-113 116-130 131-145 216-229 D E T G T E H E ++Y++ V L Q +I+ +Q+ L+V+ C +L+ +Q+ +E+ +E+ +L+ G ++F++ +V+ +V+ +Q+ S +E+ +F+ S ++F++ D G +L+P +L   T ++L++ T   +L++ A A >T> ++F++ N +++L+++ T S ++E++ V D S E

[0115] Panel B indicates the effect on binding affinity when successiveamino acid residues are deleted, either from the amino-terminus (rightside-symbols) or the carboxyl-terminus from the bottom (leftside-symbol). A (+) signifies a decrease in binding affinity, and theunderlined residues indicate which residue was the last residue to beserially deleted. Panel B. 105-113 116-130 131-145 216-229   D+ E T G T  E+ H E Y   V+ L+   Q+ I     Q++ L+   V+ C    L+++ Q++    E+++ +++E      L+++ G++    F+++ ++V        V+++    Q+++    S++++ +E   ++++F+++++++S+++ ++++F++++ D ++G     +++L    +++P    +L   +++T    +++L    T+++L    ++A     A ++T ++F     N ++L +T   S +E +V   D S E

[0116] All publications cited herein are hereby incorporated byreference to the same extent as if each publication were individuallyand specifically indicated to be incorporated by reference and were setforth in its entirety herein.

[0117] While this invention has been described with an emphasis uponpreferred embodiments, it will be obvious to those of ordinary skill inthe art that variations of the preferred embodiments can be used andthat it is intended that the invention can be practiced otherwise thanas specifically described herein. Accordingly, this invention includesall modifications encompassed within the spirit and scope of theinvention as defined by the following claims.

1 1242 1 9 PRT Artificial Sequence Synthetic 1 Tyr Asp Ile Xaa Tyr TyrXaa Xaa Glu 1 5 2 9 PRT Artificial Sequence Synthetic 2 Tyr Asp Ile XaaTyr Tyr Xaa Xaa Glu 1 5 3 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 3 Tyr Asp Ile Asn Tyr Tyr Thr SerGlu 1 5 4 18 PRT Artificial Sequence Synthetic 4 Xaa Xaa Tyr Xaa Xaa XaaSer Xaa Ile Tyr Asp Ile Xaa Tyr Tyr Xaa 1 5 10 15 Xaa Glu 5 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide 5Met Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 5 1015 Ser Glu 6 15 PRT Artificial Sequence Synthetic 6 Xaa Glu Xaa Ile XaaIle Tyr Xaa Xaa Xaa Asn Tyr Xaa Xaa Xaa 1 5 10 15 7 11 PRT ArtificialSequence Synthetic 7 Glu Xaa Ile Xaa Ile Tyr Xaa Xaa Xaa Asn Tyr 1 5 108 15 PRT Artificial Sequence Synthetic 8 Xaa Glu Xaa Ile Xaa Ile Tyr XaaXaa Xaa Asn Tyr Xaa Xaa Xaa 1 5 10 15 9 15 PRT Artificial SequenceSynthetic 9 Xaa Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Xaa Xaa Xaa1 5 10 15 10 9 PRT Artificial Sequence Description of ArtificialSequence binding peptide 10 Glu His Gln Ala Phe Leu Gln Phe Ser 1 5 1118 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 11 Leu Pro Pro Leu Tyr Ser Leu Val Phe Ile Phe Gly Phe Val GlyAsn 1 5 10 15 Met Leu 12 22 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 12 Gln Trp Asp Phe Gly Asn Thr MetCys Gln Leu Leu Thr Gly Leu Tyr 1 5 10 15 Phe Ile Gly Phe Phe Ser 20 1318 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 13 Ser Gln Tyr Gln Phe Trp Lys Asn Phe Gln Thr Leu Lys Ile ValIle 1 5 10 15 Leu Gly 14 22 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 14 Ala Pro Tyr Asn Ile Val Leu LeuLeu Asn Thr Phe Gln Glu Phe Phe 1 5 10 15 Gly Leu Asn Asn Cys Ser 20 1518 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 15 Tyr Ala Phe Val Gly Glu Lys Phe Arg Asn Tyr Leu Leu Val PhePhe 1 5 10 15 Gln Lys 16 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 16 Leu Leu Leu Thr Ile Pro Asp PheIle Phe Ala Asn Val Ser Glu Ala 1 5 10 15 Asp Asp 17 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 17 Val ValPhe Gln Phe Gln His Ile Met Val Gly Leu Ile Leu Pro Gly 1 5 10 15 IleVal 18 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 18 Ile Asp Ser Phe Ile Leu Leu Glu Ile Ile Lys Gln GlyCys Glu Phe 1 5 10 15 Glu Asn 19 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 19 Leu Val Ile Ser Ile Phe TyrHis Lys Leu Gln Ser Leu Thr Asp Val 1 5 10 15 Phe Leu 20 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide20 Pro Phe Trp Ala Tyr Ala Gly Ile His Glu Trp Val Phe Gly Gln Val 1 510 15 Met Cys 21 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 21 Glu Ala Ile Ser Thr Val Val Leu Ala Thr GlnMet Thr Leu Gly Phe 1 5 10 15 Phe Leu 22 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 22 Leu Thr Met IleVal Cys Tyr Ser Val Ile Ile Lys Thr Leu Leu His 1 5 10 15 Ala Gly 23 22PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 23 Met Ala Val Phe Leu Leu Thr Gln Met Pro Phe Asn Leu Met LysPhe 1 5 10 15 Ile Arg Ser Thr His Trp 20 24 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 24 His Trp Glu TyrTyr Ala Met Thr Ser Phe His Tyr Thr Ile Met Val 1 5 10 15 Thr Glu 25 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 25 Ala Cys Leu Asn Pro Val Leu Tyr Ala Phe Val Ser Leu Lys PheArg 1 5 10 15 Lys Asn 26 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 26 Ser Lys Thr Phe Ser Ala Ser HisAsn Val Glu Ala Thr Ser Met Phe 1 5 10 15 Gln Leu 27 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 27 Asp ThrTyr Ile Cys Glu Val Glu Asp 1 5 28 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 28 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 29 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide29 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 1530 15 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 30 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 15 10 15 31 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 31 Met Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ile AsnTyr Tyr Thr 1 5 10 15 Ser Glu 32 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 32 Val Ser Ser Pro Ile Tyr AspIle Asn Tyr Tyr Thr Ser Glu Pro Cys 1 5 10 15 Gln Lys 33 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide33 Ile Tyr Asp Ile Asn Tyr Tyr Thr Ser Glu Pro Cys Gln Lys Ile Asn 1 510 15 Val Lys 34 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 34 Asn Tyr Tyr Thr Ser Glu Pro Cys Gln Lys IleAsn Val Lys Gln Ile 1 5 10 15 Ala Ala 35 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 35 Ser Glu Pro CysGln Lys Ile Asn Val Lys Gln Ile Ala Ala Arg Leu 1 5 10 15 Leu Pro 36 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 36 Gln Lys Ile Asn Val Lys Gln Ile Ala Ala Arg Leu Leu Pro ProLeu 1 5 10 15 Tyr Ser 37 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 37 Val Lys Gln Ile Ala Ala Arg LeuLeu Pro Pro Leu Tyr Ser Leu Val 1 5 10 15 Phe Ile 38 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 38 Ala AlaArg Leu Leu Pro Pro Leu Tyr Ser Leu Val Phe Ile Phe Gly 1 5 10 15 PheVal 39 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 39 Leu Pro Pro Leu Tyr Ser Leu Val Phe Ile Phe Gly PheVal Gly Asn 1 5 10 15 Met Leu 40 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 40 Tyr Ser Leu Val Phe Ile PheGly Phe Val Gly Asn Met Leu Val Ile 1 5 10 15 Leu Ile 41 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide41 Phe Ile Phe Gly Phe Val Gly Asn Met Leu Val Ile Leu Ile Leu Ile 1 510 15 Asn Cys 42 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 42 Phe Val Gly Asn Met Leu Val Ile Leu Ile LeuIle Asn Cys Lys Arg 1 5 10 15 Leu Lys 43 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 43 Met Leu Val IleLeu Ile Leu Ile Asn Cys Lys Arg Leu Lys Ser Met 1 5 10 15 Thr Asp 44 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 44 Leu Ile Leu Ile Asn Cys Lys Arg Leu Lys Ser Met Thr Asp IleTyr 1 5 10 15 Leu Leu 45 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 45 Asn Cys Lys Arg Leu Lys Ser MetThr Asp Ile Tyr Leu Leu Asn Leu 1 5 10 15 Ala Ile 46 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 46 Leu LysSer Met Thr Asp Ile Tyr Leu Leu Asn Leu Ala Ile Ser Asp 1 5 10 15 LeuPhe 47 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 47 Thr Asp Ile Tyr Leu Leu Asn Leu Ala Ile Ser Asp LeuPhe Phe Leu 1 5 10 15 Leu Thr 48 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 48 Leu Leu Asn Leu Ala Ile SerAsp Leu Phe Phe Leu Leu Thr Val Pro 1 5 10 15 Phe Trp 49 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide49 Ala Ile Ser Asp Leu Phe Phe Leu Leu Thr Val Pro Phe Trp Ala His 1 510 15 Tyr Ala 50 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 50 Leu Phe Phe Leu Leu Thr Val Pro Phe Trp AlaHis Tyr Ala Ala Ala 1 5 10 15 Gln Trp 51 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 51 Leu Thr Val ProPhe Trp Ala His Tyr Ala Ala Ala Gln Trp Asp Phe 1 5 10 15 Gly Asn 52 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 52 Phe Trp Ala His Tyr Ala Ala Ala Gln Trp Asp Phe Gly Asn ThrMet 1 5 10 15 Cys Gln 53 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 53 Tyr Ala Ala Ala Gln Trp Asp PheGly Asn Thr Met Cys Gln Leu Leu 1 5 10 15 Thr Gly 54 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 54 Gln TrpAsp Phe Gly Asn Thr Met Cys Gln Leu Leu Thr Gly Leu Tyr 1 5 10 15 PheIle 55 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 55 Gly Asn Thr Met Cys Gln Leu Leu Thr Gly Leu Tyr PheIle Gly Phe 1 5 10 15 Phe Ser 56 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 56 Cys Gln Leu Leu Thr Gly LeuTyr Phe Ile Gly Phe Phe Ser Gly Ile 1 5 10 15 Phe Phe 57 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide57 Thr Gly Leu Tyr Phe Ile Gly Phe Phe Ser Gly Ile Phe Phe Ile Ile 1 510 15 Leu Leu 58 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 58 Phe Ile Gly Phe Phe Ser Gly Ile Phe Phe IleIle Leu Leu Thr Ile 1 5 10 15 Asp Arg 59 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 59 Phe Ser Gly IlePhe Phe Ile Ile Leu Leu Thr Ile Asp Arg Tyr Leu 1 5 10 15 Ala Val 60 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 60 Phe Phe Ile Ile Leu Leu Thr Ile Asp Arg Tyr Leu Ala Val ValHis 1 5 10 15 Ala Val 61 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 61 Leu Leu Thr Ile Asp Arg Tyr LeuAla Val Val His Ala Val Phe Ala 1 5 10 15 Leu Lys 62 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 62 Asp ArgTyr Leu Ala Val Val His Ala Val Phe Ala Leu Lys Ala Arg 1 5 10 15 ThrVal 63 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 63 Ala Val Val His Ala Val Phe Ala Leu Lys Ala Arg ThrVal Thr Phe 1 5 10 15 Gly Val 64 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 64 Ala Val Phe Ala Leu Lys AlaArg Thr Val Thr Phe Gly Val Val Thr 1 5 10 15 Ser Val 65 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide65 Leu Lys Ala Arg Thr Val Thr Phe Gly Val Val Thr Ser Val Ile Thr 1 510 15 Trp Val 66 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 66 Thr Val Thr Phe Gly Val Val Thr Ser Val IleThr Trp Val Val Ala 1 5 10 15 Val Phe 67 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 67 Gly Val Val ThrSer Val Ile Thr Trp Val Val Ala Val Phe Ala Ser 1 5 10 15 Leu Pro 68 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 68 Ser Val Ile Thr Trp Val Val Ala Val Phe Ala Ser Leu Pro GlyIle 1 5 10 15 Ile Phe 69 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 69 Trp Val Val Ala Val Phe Ala SerLeu Pro Gly Ile Ile Phe Thr Arg 1 5 10 15 Ser Gln 70 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 70 Val PheAla Ser Leu Pro Gly Ile Ile Phe Thr Arg Ser Gln Lys Glu 1 5 10 15 GlyLeu 71 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 71 Leu Pro Gly Ile Ile Phe Thr Arg Ser Gln Lys Glu GlyLeu His Tyr 1 5 10 15 Thr Cys 72 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 72 Ile Phe Thr Arg Ser Gln LysGlu Gly Leu His Tyr Thr Cys Ser Ser 1 5 10 15 His Phe 73 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide73 Ser Gln Lys Glu Gly Leu His Tyr Thr Cys Ser Ser His Phe Pro Tyr 1 510 15 Ser Gln 74 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 74 Gly Leu His Tyr Thr Cys Ser Ser His Phe ProTyr Ser Gln Tyr Gln 1 5 10 15 Phe Trp 75 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 75 Gly Leu His TyrThr Cys Ser Ser His Phe Pro Tyr Ser Gln Tyr Gln 1 5 10 15 Phe Trp 76 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 76 His Phe Pro Tyr Ser Gln Tyr Gln Phe Trp Lys Asn Phe Gln ThrLeu 1 5 10 15 Lys Ile 77 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 77 Ser Gln Tyr Gln Phe Trp Lys AsnPhe Gln Thr Leu Lys Ile Val Ile 1 5 10 15 Leu Gly 78 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 78 Phe TrpLys Asn Phe Gln Thr Leu Lys Ile Val Ile Leu Gly Leu Val 1 5 10 15 LeuPro 79 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 79 Phe Gln Thr Leu Lys Ile Val Ile Leu Gly Leu Val LeuPro Leu Leu 1 5 10 15 Val Met 80 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 80 Lys Ile Val Ile Leu Gly LeuVal Leu Pro Leu Leu Val Met Val Ile 1 5 10 15 Cys Tyr 81 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide81 Leu Gly Leu Val Leu Pro Leu Leu Val Met Val Ile Cys Tyr Ser Gly 1 510 15 Ile Leu 82 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 82 Leu Pro Leu Leu Val Met Val Ile Cys Tyr SerGly Ile Leu Lys Thr 1 5 10 15 Leu Leu 83 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 83 Val Met Val IleCys Tyr Ser Gly Ile Leu Lys Thr Leu Leu Arg Cys 1 5 10 15 Arg Asn 84 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 84 Cys Tyr Ser Gly Ile Leu Lys Thr Leu Leu Arg Cys Arg Asn GluLys 1 5 10 15 Lys Arg 85 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 85 Ile Leu Lys Thr Leu Leu Arg CysArg Asn Glu Lys Lys Arg His Arg 1 5 10 15 Ala Val 86 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 86 Leu LeuArg Cys Arg Asn Glu Lys Lys Arg His Arg Ala Val Arg Leu 1 5 10 15 IlePhe 87 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 87 Arg Asn Glu Lys Lys Arg His Arg Ala Val Arg Leu IlePhe Thr Ile 1 5 10 15 Met Ile 88 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 88 Lys Arg His Arg Ala Val ArgLeu Ile Phe Thr Ile Met Ile Val Tyr 1 5 10 15 Phe Leu 89 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide89 Ala Val Arg Leu Ile Phe Thr Ile Met Ile Val Tyr Phe Leu Phe Trp 1 510 15 Ala Pro 90 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 90 Ile Phe Thr Ile Met Ile Val Tyr Phe Leu PheTrp Ala Pro Tyr Asn 1 5 10 15 Ile Val 91 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 91 Met Ile Val TyrPhe Leu Phe Trp Ala Pro Tyr Asn Ile Val Leu Leu 1 5 10 15 Leu Asn 92 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 92 Phe Leu Phe Trp Ala Pro Tyr Asn Ile Val Leu Leu Leu Asn ThrPhe 1 5 10 15 Gln Glu 93 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 93 Ala Pro Tyr Asn Ile Val Leu LeuLeu Asn Thr Phe Gln Glu Phe Phe 1 5 10 15 Gly Leu 94 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 94 Ile ValLeu Leu Leu Asn Thr Phe Gln Glu Phe Phe Gly Leu Asn Asn 1 5 10 15 CysSer 95 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 95 Leu Asn Thr Phe Gln Glu Phe Phe Gly Leu Asn Asn CysSer Ser Ser 1 5 10 15 Asn Arg 96 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 96 Gln Glu Phe Phe Gly Leu AsnAsn Cys Ser Ser Ser Asn Arg Leu Asp 1 5 10 15 Gln Ala 97 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide97 Gly Leu Asn Asn Cys Ser Ser Ser Asn Arg Leu Asp Gln Ala Met Gln 1 510 15 Val Thr 98 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 98 Cys Ser Ser Ser Asn Arg Leu Asp Gln Ala MetGln Val Thr Glu Thr 1 5 10 15 Leu Gly 99 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 99 Asn Arg Leu AspGln Ala Met Gln Val Thr Glu Thr Leu Gly Met Thr 1 5 10 15 His Cys 100 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 100 Gln Ala Met Gln Val Thr Glu Thr Leu Gly Met Thr His Cys CysIle 1 5 10 15 Asn Pro 101 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 101 Val Thr Glu Thr Leu Gly Met ThrHis Cys Cys Ile Asn Pro Ile Ile 1 5 10 15 Tyr Ala 102 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 102 Leu GlyMet Thr His Cys Cys Ile Asn Pro Ile Ile Tyr Ala Phe Val 1 5 10 15 GlyGlu 103 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 103 His Cys Cys Ile Asn Pro Ile Ile Tyr Ala Phe Val GlyGlu Lys Phe 1 5 10 15 Arg Asn 104 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 104 Asn Pro Ile Ile Tyr Ala PheVal Gly Glu Lys Phe Arg Asn Tyr Leu 1 5 10 15 Leu Val 105 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide105 Tyr Ala Phe Val Gly Glu Lys Phe Arg Asn Tyr Leu Leu Val Phe Phe 1 510 15 Gln Lys 106 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 106 Gly Glu Lys Phe Arg Asn Tyr Leu Leu Val PhePhe Gln Lys His Ile 1 5 10 15 Ala Lys 107 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 107 Arg Asn Tyr LeuLeu Val Phe Phe Gln Lys His Ile Ala Lys Arg Phe 1 5 10 15 Cys Lys 108 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 108 Leu Val Phe Phe Gln Lys His Ile Ala Lys Arg Phe Cys Lys CysCys 1 5 10 15 Ser Ile 109 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 109 Gln Lys His Ile Ala Lys Arg PheCys Lys Cys Cys Ser Ile Phe Gln 1 5 10 15 Gln Glu 110 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 110 Ala LysArg Phe Cys Lys Cys Cys Ser Ile Phe Gln Gln Glu Ala Pro 1 5 10 15 GluArg 111 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 111 Cys Lys Cys Cys Ser Ile Phe Gln Gln Glu Ala Pro GluArg Ala Ser 1 5 10 15 Ser Val 112 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 112 Ser Ile Phe Gln Gln Glu AlaPro Glu Arg Ala Ser Ser Val Tyr Thr 1 5 10 15 Arg Ser 113 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide113 Gln Glu Ala Pro Glu Arg Ala Ser Ser Val Tyr Thr Arg Ser Thr Gly 1 510 15 Glu Gln 114 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 114 Glu Arg Ala Ser Ser Val Tyr Thr Arg Ser ThrGly Glu Gln Glu Ile 1 5 10 15 Ser Val 115 16 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 115 Ser Val Tyr ThrArg Ser Thr Gly Glu Gln Glu Ile Ser Val Gly Leu 1 5 10 15 116 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide116 Met Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met 1 510 15 Gly Ser 117 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 117 Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu GluMet Gly Ser Gly Asp 1 5 10 15 Tyr Asp 118 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 118 Ser Asp Asn TyrThr Glu Glu Met Gly Ser Gly Asp Tyr Asp Ser Met 1 5 10 15 Lys Glu 119 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 119 Thr Glu Glu Met Gly Ser Gly Asp Tyr Asp Ser Met Lys Glu ProCys 1 5 10 15 Phe Arg 120 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 120 Gly Ser Gly Asp Tyr Asp Ser MetLys Glu Pro Cys Phe Arg Glu Glu 1 5 10 15 Asn Ala 121 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 121 Tyr AspSer Met Lys Glu Pro Cys Phe Arg Glu Glu Asn Ala Asn Phe 1 5 10 15 AsnLys 122 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 122 Lys Glu Pro Cys Phe Arg Glu Glu Asn Ala Asn Phe AsnLys Ile Phe 1 5 10 15 Leu Pro 123 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 123 Phe Arg Glu Glu Asn Ala AsnPhe Asn Lys Ile Phe Leu Pro Thr Ile 1 5 10 15 Tyr Ser 124 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide124 Asn Ala Asn Phe Asn Lys Ile Phe Leu Pro Thr Ile Tyr Ser Ile Ile 1 510 15 Phe Leu 125 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 125 Asn Lys Ile Phe Leu Pro Thr Ile Tyr Ser IleIle Phe Leu Thr Gly 1 5 10 15 Ile Val 126 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 126 Leu Pro Thr IleTyr Ser Ile Ile Phe Leu Thr Gly Ile Val Gly Asn 1 5 10 15 Gly Leu 127 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 127 Tyr Ser Ile Ile Phe Leu Thr Gly Ile Val Gly Asn Gly Leu ValIle 1 5 10 15 Leu Val 128 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 128 Phe Leu Thr Gly Ile Val Gly AsnGly Leu Val Ile Leu Val Met Gly 1 5 10 15 Tyr Gln 129 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 129 Ile ValGly Asn Gly Leu Val Ile Leu Val Met Gly Tyr Gln Lys Lys 1 5 10 15 LeuArg 130 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 130 Gly Leu Val Ile Leu Val Met Gly Tyr Gln Lys Lys LeuArg Ser Met 1 5 10 15 Thr Asp 131 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 131 Leu Val Met Gly Tyr Gln LysLys Leu Arg Ser Met Thr Asp Lys Tyr 1 5 10 15 Arg Leu 132 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide132 Tyr Gln Lys Lys Leu Arg Ser Met Thr Asp Lys Tyr Arg Leu His Leu 1 510 15 Ser Val 133 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 133 Leu Arg Ser Met Thr Asp Lys Tyr Arg Leu HisLeu Ser Val Ala Asp 1 5 10 15 Leu Leu 134 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 134 Thr Asp Lys TyrArg Leu His Leu Ser Val Ala Asp Leu Leu Phe Val 1 5 10 15 Ile Thr 135 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 135 Arg Leu His Leu Ser Val Ala Asp Leu Leu Phe Val Ile Thr LeuPro 1 5 10 15 Phe Trp 136 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 136 Ser Val Ala Asp Leu Leu Phe ValIle Thr Leu Pro Phe Trp Ala Val 1 5 10 15 Asp Ala 137 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 137 Leu LeuPhe Val Ile Thr Leu Pro Phe Trp Ala Val Asp Ala Val Ala 1 5 10 15 AsnTrp 138 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 138 Ile Thr Leu Pro Phe Trp Ala Val Asp Ala Val Ala AsnTrp Tyr Phe 1 5 10 15 Gly Asn 139 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 139 Phe Trp Ala Val Asp Ala ValAla Asn Trp Tyr Phe Gly Asn Phe Leu 1 5 10 15 Cys Lys 140 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide140 Asp Ala Val Ala Asn Trp Tyr Phe Gly Asn Phe Leu Cys Lys Ala Val 1 510 15 His Val 141 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 141 Asn Trp Tyr Phe Gly Asn Phe Leu Cys Lys AlaVal His Val Ile Tyr 1 5 10 15 Thr Val 142 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 142 Gly Asn Phe LeuCys Lys Ala Val His Val Ile Tyr Thr Val Asn Leu 1 5 10 15 Tyr Ser 143 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 143 Cys Lys Ala Val His Val Ile Tyr Thr Val Asn Leu Tyr Ser SerVal 1 5 10 15 Leu Ile 144 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 144 His Val Ile Tyr Thr Val Asn LeuTyr Ser Ser Val Leu Ile Leu Ala 1 5 10 15 Phe Ile 145 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 145 Thr ValAsn Leu Tyr Ser Ser Val Leu Ile Leu Ala Phe Ile Ser Leu 1 5 10 15 AspArg 146 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 146 Tyr Ser Ser Val Leu Ile Leu Ala Phe Ile Ser Leu AspArg Tyr Leu 1 5 10 15 Ala Ile 147 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 147 Leu Ile Leu Ala Phe Ile SerLeu Asp Arg Tyr Leu Ala Ile Val His 1 5 10 15 Ala Thr 148 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide148 Phe Ile Ser Leu Asp Arg Tyr Leu Ala Ile Val His Ala Thr Asn Ser 1 510 15 Gln Arg 149 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 149 Asp Arg Tyr Leu Ala Ile Val His Ala Thr AsnSer Gln Arg Pro Arg 1 5 10 15 Lys Leu 150 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 150 Ala Ile Val HisAla Thr Asn Ser Gln Arg Pro Arg Lys Leu Leu Ala 1 5 10 15 Glu Lys 151 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 151 Ala Thr Asn Ser Gln Arg Pro Arg Lys Leu Leu Ala Glu Lys ValVal 1 5 10 15 Tyr Val 152 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 152 Gln Arg Pro Arg Lys Leu Leu AlaGlu Lys Val Val Tyr Val Gly Val 1 5 10 15 Trp Ile 153 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 153 Lys LeuLeu Ala Glu Lys Val Val Tyr Val Gly Val Trp Ile Pro Ala 1 5 10 15 LeuLeu 154 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 154 Glu Lys Val Val Tyr Val Gly Val Trp Ile Pro Ala LeuLeu Leu Thr 1 5 10 15 Ile Pro 155 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 155 Tyr Val Gly Val Trp Ile ProAla Leu Leu Leu Thr Ile Pro Asp Phe 1 5 10 15 Ile Phe 156 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide156 Trp Ile Pro Ala Leu Leu Leu Thr Ile Pro Asp Phe Ile Phe Ala Asn 1 510 15 Val Ser 157 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 157 Leu Leu Leu Thr Ile Pro Asp Phe Ile Phe AlaAsn Val Ser Glu Ala 1 5 10 15 Asp Asp 158 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 158 Ile Pro Asp PheIle Phe Ala Asn Val Ser Glu Ala Asp Asp Arg Tyr 1 5 10 15 Ile Cys 159 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 159 Ile Phe Ala Asn Val Ser Glu Ala Asp Asp Arg Tyr Ile Cys AspArg 1 5 10 15 Phe Tyr 160 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 160 Val Ser Glu Ala Asp Asp Arg TyrIle Cys Asp Arg Phe Tyr Pro Asn 1 5 10 15 Asp Leu 161 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 161 Asp AspArg Tyr Ile Cys Asp Arg Phe Tyr Pro Asn Asp Leu Trp Val 1 5 10 15 ValVal 162 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 162 Ile Cys Asp Arg Phe Tyr Pro Asn Asp Leu Trp Val ValVal Phe Gln 1 5 10 15 Phe Gln 163 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 163 Phe Tyr Pro Asn Asp Leu TrpVal Val Val Phe Gln Phe Gln His Ile 1 5 10 15 Met Val 164 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide164 Asp Leu Trp Val Val Val Phe Gln Phe Gln His Ile Met Val Gly Leu 1 510 15 Ile Leu 165 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 165 Val Val Phe Gln Phe Gln His Ile Met Val GlyLeu Ile Leu Pro Gly 1 5 10 15 Ile Val 166 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 166 Phe Gln His IleMet Val Gly Leu Ile Leu Pro Gly Ile Val Ile Leu 1 5 10 15 Ser Cys 167 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 167 Met Val Gly Leu Ile Leu Pro Gly Ile Val Ile Leu Ser Cys TyrCys 1 5 10 15 Ile Ile 168 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 168 Ile Leu Pro Gly Ile Val Ile LeuSer Cys Tyr Cys Ile Ile Ile Ser 1 5 10 15 Lys Leu 169 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 169 Ile ValIle Leu Ser Cys Tyr Cys Ile Ile Ile Ser Lys Leu Ser His 1 5 10 15 SerLys 170 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 170 Ser Cys Tyr Cys Ile Ile Ile Ser Lys Leu Ser His SerLys Gly His 1 5 10 15 Gln Lys 171 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 171 Ile Ile Ile Ser Lys Leu SerHis Ser Lys Gly His Gln Lys Arg Lys 1 5 10 15 Ala Leu 172 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide172 Lys Leu Ser His Ser Lys Gly His Gln Lys Arg Lys Ala Leu Lys Thr 1 510 15 Thr Val 173 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 173 Ser Lys Gly His Gln Lys Arg Lys Ala Leu LysThr Thr Val Ile Leu 1 5 10 15 Ile Leu 174 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 174 Gln Lys Arg LysAla Leu Lys Thr Thr Val Ile Leu Ile Leu Ala Phe 1 5 10 15 Phe Ala 175 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 175 Ala Leu Lys Thr Thr Val Ile Leu Ile Leu Ala Phe Phe Ala CysTrp 1 5 10 15 Leu Pro 176 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 176 Thr Val Ile Leu Ile Leu Ala PhePhe Ala Cys Trp Leu Pro Tyr Tyr 1 5 10 15 Ile Gly 177 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 177 Ile LeuAla Phe Phe Ala Cys Trp Leu Pro Tyr Tyr Ile Gly Ile Ser 1 5 10 15 IleAsp 178 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 178 Phe Ala Cys Trp Leu Pro Tyr Tyr Ile Gly Ile Ser IleAsp Ser Phe 1 5 10 15 Ile Leu 179 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 179 Leu Pro Tyr Tyr Ile Gly IleSer Ile Asp Ser Phe Ile Leu Leu Glu 1 5 10 15 Ile Ile 180 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide180 Ile Gly Ile Ser Ile Asp Ser Phe Ile Leu Leu Glu Ile Ile Lys Gln 1 510 15 Gly Cys 181 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 181 Ile Asp Ser Phe Ile Leu Leu Glu Ile Ile LysGln Gly Cys Glu Phe 1 5 10 15 Glu Asn 182 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 182 Ile Leu Leu GluIle Ile Lys Gln Gly Cys Glu Phe Glu Asn Thr Val 1 5 10 15 His Lys 183 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 183 Ile Ile Lys Gln Gly Cys Glu Phe Glu Asn Thr Val His Lys TrpIle 1 5 10 15 Ser Ile 184 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 184 Gly Cys Glu Phe Glu Asn Thr ValHis Lys Trp Ile Ser Ile Thr Glu 1 5 10 15 Ala Leu 185 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 185 Glu AsnThr Val His Lys Trp Ile Ser Ile Thr Glu Ala Leu Ala Phe 1 5 10 15 PheHis 186 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 186 His Lys Trp Ile Ser Ile Thr Glu Ala Leu Ala Phe PheHis Cys Cys 1 5 10 15 Leu Asn 187 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 187 Ser Ile Thr Glu Ala Leu AlaPhe Phe His Cys Cys Leu Asn Pro Ile 1 5 10 15 Leu Tyr 188 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide188 Ala Leu Ala Phe Phe His Cys Cys Leu Asn Pro Ile Leu Tyr Ala Phe 1 510 15 Leu Gly 189 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 189 Phe His Cys Cys Leu Asn Pro Ile Leu Tyr AlaPhe Leu Gly Ala Lys 1 5 10 15 Phe Lys 190 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 190 Leu Asn Pro IleLeu Tyr Ala Phe Leu Gly Ala Lys Phe Lys Thr Ser 1 5 10 15 Ala Gln 191 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 191 Leu Tyr Ala Phe Leu Gly Ala Lys Phe Lys Thr Ser Ala Gln HisAla 1 5 10 15 Leu Thr 192 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 192 Leu Gly Ala Lys Phe Lys Thr SerAla Gln His Ala Leu Thr Ser Val 1 5 10 15 Ser Arg 193 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 193 Phe LysThr Ser Ala Gln His Ala Leu Thr Ser Val Ser Arg Gly Ser 1 5 10 15 SerLeu 194 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 194 Ala Gln His Ala Leu Thr Ser Val Ser Arg Gly Ser SerLeu Lys Ile 1 5 10 15 Leu Ser 195 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 195 Leu Thr Ser Val Ser Arg GlySer Ser Leu Lys Ile Leu Ser Lys Gly 1 5 10 15 Lys Arg 196 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide196 Ser Arg Gly Ser Ser Leu Lys Ile Leu Ser Lys Gly Lys Arg Gly Gly 1 510 15 His Ser 197 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 197 Ser Leu Lys Ile Leu Ser Lys Gly Lys Arg GlyGly His Ser Ser Val 1 5 10 15 Ser Thr 198 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 198 Leu Ser Lys GlyLys Arg Gly Gly His Ser Ser Val Ser Thr Glu Ser 1 5 10 15 Glu Ser 199 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 199 Lys Arg Gly Gly His Ser Ser Val Ser Thr Glu Ser Glu Ser SerSer 1 5 10 15 Phe His 200 16 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 200 His Ser Ser Val Ser Thr Glu SerGlu Ser Ser Ser Phe His Ser Ser 1 5 10 15 201 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 201 Met Ala Glu HisAsp Tyr His Glu Asp Tyr Gly Phe Ser Ser Phe Asn 1 5 10 15 Asp Ser 202 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 202 Asp Tyr His Glu Asp Tyr Gly Phe Ser Ser Phe Asn Asp Ser SerGln 1 5 10 15 Glu Glu 203 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 203 Asp Tyr Gly Phe Ser Ser Phe AsnAsp Ser Ser Gln Glu Glu His Gln 1 5 10 15 Ala Phe 204 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 204 Ser SerPhe Asn Asp Ser Ser Gln Glu Glu His Gln Ala Phe Leu Gln 1 5 10 15 PheSer 205 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 205 Asp Ser Ser Gln Glu Glu His Gln Ala Phe Leu Gln PheSer Lys Val 1 5 10 15 Phe Leu 206 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 206 Glu Glu His Gln Ala Phe LeuGln Phe Ser Lys Val Phe Leu Pro Cys 1 5 10 15 Met Tyr 207 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide207 Ala Phe Leu Gln Phe Ser Lys Val Phe Leu Pro Cys Met Tyr Leu Val 1 510 15 Val Phe 208 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 208 Phe Ser Lys Val Phe Leu Pro Cys Met Tyr LeuVal Val Phe Val Cys 1 5 10 15 Gly Leu 209 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 209 Phe Leu Pro CysMet Tyr Leu Val Val Phe Val Cys Gly Leu Val Gly 1 5 10 15 Asn Ser 210 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 210 Met Tyr Leu Val Val Phe Val Cys Gly Leu Val Gly Asn Ser LeuVal 1 5 10 15 Leu Val 211 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 211 Val Phe Val Cys Gly Leu Val GlyAsn Ser Leu Val Leu Val Ile Ser 1 5 10 15 Ile Phe 212 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 212 Gly LeuVal Gly Asn Ser Leu Val Leu Val Ile Ser Ile Phe Tyr His 1 5 10 15 LysLeu 213 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 213 Asn Ser Leu Val Leu Val Ile Ser Ile Phe Tyr His LysLeu Gln Ser 1 5 10 15 Leu Thr 214 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 214 Leu Val Ile Ser Ile Phe TyrHis Lys Leu Gln Ser Leu Thr Asp Val 1 5 10 15 Phe Leu 215 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide215 Ile Phe Tyr His Lys Leu Gln Ser Leu Thr Asp Val Phe Leu Val Asn 1 510 15 Leu Pro 216 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 216 Lys Leu Gln Ser Leu Thr Asp Val Phe Leu ValAsn Leu Pro Leu Ala 1 5 10 15 Asp Leu 217 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 217 Leu Thr Asp ValPhe Leu Val Asn Leu Pro Leu Ala Asp Leu Val Phe 1 5 10 15 Val Cys 218 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 218 Phe Leu Val Asn Leu Pro Leu Ala Asp Leu Val Phe Val Cys ThrLeu 1 5 10 15 Pro Phe 219 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 219 Leu Pro Leu Ala Asp Leu Val PheVal Cys Thr Leu Pro Phe Trp Ala 1 5 10 15 Tyr Ala 220 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 220 Asp LeuVal Phe Val Cys Thr Leu Pro Phe Trp Ala Tyr Ala Gly Ile 1 5 10 15 HisGlu 221 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 221 Val Cys Thr Leu Pro Phe Trp Ala Tyr Ala Gly Ile HisGlu Trp Val 1 5 10 15 Phe Gly 222 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 222 Pro Phe Trp Ala Tyr Ala GlyIle His Glu Trp Val Phe Gly Gln Val 1 5 10 15 Met Cys 223 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide223 Pro Phe Trp Ala Tyr Ala Gly Ile His Glu Trp Val Phe Gly Gln Val 1 510 15 Met Cys 224 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 224 His Glu Trp Val Phe Gly Gln Val Met Cys LysSer Leu Leu Gly Ile 1 5 10 15 Tyr Thr 225 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 225 Phe Gly Gln ValMet Cys Lys Ser Leu Leu Gly Ile Tyr Thr Ile Asn 1 5 10 15 Phe Tyr 226 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 226 Met Cys Lys Ser Leu Leu Gly Ile Tyr Thr Ile Asn Phe Tyr ThrSer 1 5 10 15 Met Leu 227 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 227 Leu Leu Gly Ile Tyr Thr Ile AsnPhe Tyr Thr Ser Met Leu Ile Leu 1 5 10 15 Thr Cys 228 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 228 Tyr ThrIle Asn Phe Tyr Thr Ser Met Leu Ile Leu Thr Cys Ile Thr 1 5 10 15 ValAsp 229 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 229 Phe Tyr Thr Ser Met Leu Ile Leu Thr Cys Ile Thr ValAsp Arg Phe 1 5 10 15 Ile Val 230 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 230 Met Leu Ile Leu Thr Cys IleThr Val Asp Arg Phe Ile Val Val Val 1 5 10 15 Lys Ala 231 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide231 Thr Cys Ile Thr Val Asp Arg Phe Ile Val Val Val Lys Ala Thr Lys 1 510 15 Ala Tyr 232 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 232 Val Asp Arg Phe Ile Val Val Val Lys Ala ThrLys Ala Tyr Asn Gln 1 5 10 15 Gln Ala 233 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 233 Ile Val Val ValLys Ala Thr Lys Ala Tyr Asn Gln Gln Ala Lys Arg 1 5 10 15 Met Thr 234 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 234 Lys Ala Thr Lys Ala Tyr Asn Gln Gln Ala Lys Arg Met Thr TrpGly 1 5 10 15 Lys Val 235 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 235 Ala Tyr Asn Gln Gln Ala Lys ArgMet Thr Trp Gly Lys Val Thr Ser 1 5 10 15 Leu Leu 236 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 236 Gln AlaLys Arg Met Thr Trp Gly Lys Val Thr Ser Leu Leu Ile Trp 1 5 10 15 ValIle 237 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 237 Met Thr Trp Gly Lys Val Thr Ser Leu Leu Ile Trp ValIle Ser Leu 1 5 10 15 Leu Val 238 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 238 Lys Val Thr Ser Leu Leu IleTrp Val Ile Ser Leu Leu Val Ser Leu 1 5 10 15 Pro Gln 239 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide239 Leu Leu Ile Trp Val Ile Ser Leu Leu Val Ser Leu Pro Gln Ile Ile 1 510 15 Tyr Gly 240 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 240 Val Ile Ser Leu Leu Val Ser Leu Pro Gln IleIle Tyr Gly Asn Val 1 5 10 15 Phe Asn 241 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 241 Leu Val Ser LeuPro Gln Ile Ile Tyr Gly Asn Val Phe Asn Leu Asp 1 5 10 15 Lys Leu 242 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 242 Pro Gln Ile Ile Tyr Gly Asn Val Phe Asn Leu Asp Lys Leu IleCys 1 5 10 15 Gly Tyr 243 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 243 Tyr Gly Asn Val Phe Asn Leu AspLys Leu Ile Cys Gly Tyr His Asp 1 5 10 15 Glu Ala 244 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 244 Phe AsnLeu Asp Lys Leu Ile Cys Gly Tyr His Asp Glu Ala Ile Ser 1 5 10 15 ThrVal 245 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 245 Lys Leu Ile Cys Gly Tyr His Asp Glu Ala Ile Ser ThrVal Val Leu 1 5 10 15 Ala Thr 246 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 246 Gly Tyr His Asp Glu Ala IleSer Thr Val Val Leu Ala Thr Gln Met 1 5 10 15 Thr Leu 247 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide247 Glu Ala Ile Ser Thr Val Val Leu Ala Thr Gln Met Thr Leu Gly Phe 1 510 15 Phe Leu 248 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 248 Thr Val Val Leu Ala Thr Gln Met Thr Leu GlyPhe Phe Leu Pro Leu 1 5 10 15 Leu Thr 249 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 249 Ala Thr Gln MetThr Leu Gly Phe Phe Leu Pro Leu Leu Thr Met Ile 1 5 10 15 Val Cys 250 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 250 Thr Leu Gly Phe Phe Leu Pro Leu Leu Thr Met Ile Val Cys TyrSer 1 5 10 15 Val Ile 251 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 251 Phe Leu Pro Leu Leu Thr Met IleVal Cys Tyr Ser Val Ile Ile Lys 1 5 10 15 Thr Leu 252 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 252 Leu ThrMet Ile Val Cys Tyr Ser Val Ile Ile Lys Thr Leu Leu His 1 5 10 15 AlaGly 253 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 253 Val Cys Tyr Ser Val Ile Ile Lys Thr Leu Leu His AlaGly Gly Phe 1 5 10 15 Gln Lys 254 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 254 Val Ile Ile Lys Thr Leu LeuHis Ala Gly Gly Phe Gln Lys His Arg 1 5 10 15 Ser Leu 255 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide255 Thr Leu Leu His Ala Gly Gly Phe Gln Lys His Arg Ser Leu Lys Ile 1 510 15 Ile Phe 256 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 256 Ala Gly Gly Phe Gln Lys His Arg Ser Leu LysIle Ile Phe Leu Val 1 5 10 15 Met Ala 257 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 257 Gln Lys His ArgSer Leu Lys Ile Ile Phe Leu Val Met Ala Val Phe 1 5 10 15 Leu Leu 258 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 258 Ser Leu Lys Ile Ile Phe Leu Val Met Ala Val Phe Leu Leu ThrGln 1 5 10 15 Met Pro 259 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 259 Ile Phe Leu Val Met Ala Val PheLeu Leu Thr Gln Met Pro Phe Asn 1 5 10 15 Leu Met 260 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 260 Met AlaVal Phe Leu Leu Thr Gln Met Pro Phe Asn Leu Met Lys Phe 1 5 10 15 IleArg 261 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 261 Leu Leu Thr Gln Met Pro Phe Asn Leu Met Lys Phe IleArg Ser Thr 1 5 10 15 His Trp 262 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 262 Met Pro Phe Asn Leu Met LysPhe Ile Arg Ser Thr His Trp Glu Tyr 1 5 10 15 Tyr Ala 263 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide263 Leu Met Lys Phe Ile Arg Ser Thr His Trp Glu Tyr Tyr Ala Met Thr 1 510 15 Ser Phe 264 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 264 Ile Arg Ser Thr His Trp Glu Tyr Tyr Ala MetThr Ser Phe His Tyr 1 5 10 15 Thr Ile 265 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 265 His Trp Glu TyrTyr Ala Met Thr Ser Phe His Tyr Thr Ile Met Val 1 5 10 15 Thr Glu 266 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 266 Tyr Ala Met Thr Ser Phe His Tyr Thr Ile Met Val Thr Glu AlaIle 1 5 10 15 Ala Tyr 267 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 267 Ser Phe His Tyr Thr Ile Met ValThr Glu Ala Ile Ala Tyr Leu Arg 1 5 10 15 Ala Cys 268 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 268 Thr IleMet Val Thr Glu Ala Ile Ala Tyr Leu Arg Ala Cys Leu Asn 1 5 10 15 ProVal 269 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 269 Thr Glu Ala Ile Ala Tyr Leu Arg Ala Cys Leu Asn ProVal Leu Tyr 1 5 10 15 Ala Phe 270 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 270 Ala Tyr Leu Arg Ala Cys LeuAsn Pro Val Leu Tyr Ala Phe Val Ser 1 5 10 15 Leu Lys 271 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide271 Ala Cys Leu Asn Pro Val Leu Tyr Ala Phe Val Ser Leu Lys Phe Arg 1 510 15 Lys Asn 272 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 272 Pro Val Leu Tyr Ala Phe Val Ser Leu Lys PheArg Lys Asn Phe Trp 1 5 10 15 Lys Leu 273 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 273 Ala Phe Val SerLeu Lys Phe Arg Lys Asn Phe Trp Lys Leu Val Lys 1 5 10 15 Asp Ile 274 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 274 Leu Lys Phe Arg Lys Asn Phe Trp Lys Leu Val Lys Asp Ile GlyCys 1 5 10 15 Leu Pro 275 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 275 Lys Asn Phe Trp Lys Leu Val LysAsp Ile Gly Cys Leu Pro Tyr Leu 1 5 10 15 Gly Val 276 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 276 Lys LeuVal Lys Asp Ile Gly Cys Leu Pro Tyr Leu Gly Val Ser His 1 5 10 15 GlnTrp 277 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 277 Asp Ile Gly Cys Leu Pro Tyr Leu Gly Val Ser His GlnTrp Lys Ser 1 5 10 15 Ser Glu 278 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 278 Leu Pro Tyr Leu Gly Val SerHis Gln Trp Lys Ser Ser Glu Asp Asn 1 5 10 15 Ser Lys 279 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide279 Gly Val Ser His Gln Trp Lys Ser Ser Glu Asp Asn Ser Lys Thr Phe 1 510 15 Ser Ala 280 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 280 Gln Trp Lys Ser Ser Glu Asp Asn Ser Lys ThrPhe Ser Ala Ser His 1 5 10 15 Asn Val 281 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 281 Ser Glu Asp AsnSer Lys Thr Phe Ser Ala Ser His Asn Val Glu Ala 1 5 10 15 Thr Ser 282 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 282 Ser Lys Thr Phe Ser Ala Ser His Asn Val Glu Ala Thr Ser MetPhe 1 5 10 15 Gln Leu 283 21 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 283 Met Asn Arg Gly Val Pro Phe ArgHis Leu Leu Leu Val Leu Gln Leu 1 5 10 15 Ala Leu Leu Pro Ala 20 284 21PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 284 Pro Phe Arg His Leu Leu Leu Val Leu Gln Leu Ala Leu Leu ProAla 1 5 10 15 Ala Thr Gln Gly Lys 20 285 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 285 Leu Leu Val LeuGln Leu Ala Leu Leu Pro Ala Ala Thr Gln Gly Lys 1 5 10 15 Lys Val ValLeu Gly 20 286 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 286 Leu Ala Leu Leu Pro Ala Ala Thr Gln Gly LysLys Val Val Leu Gly 1 5 10 15 Lys Lys Gly Asp Thr 20 287 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide287 Ala Ala Thr Gln Gly Lys Lys Val Val Leu Gly Lys Lys Gly Asp Thr 1 510 15 Val Glu Leu Thr Cys 20 288 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 288 Lys Lys Val Val Leu Gly LysLys Gly Asp Thr Val Glu Leu Thr Cys 1 5 10 15 Thr Ala Ser Gln Lys 20 28921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 289 Gly Lys Lys Gly Asp Thr Val Glu Leu Thr Cys Thr Ala Ser GlnLys 1 5 10 15 Lys Ser Ile Gln Phe 20 290 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 290 Thr Val Glu LeuThr Cys Thr Ala Ser Gln Lys Lys Ser Ile Gln Phe 1 5 10 15 His Trp LysAsn Ser 20 291 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 291 Cys Thr Ala Ser Gln Lys Lys Ser Ile Gln PheHis Trp Lys Asn Ser 1 5 10 15 Asn Gln Ile Lys Ile 20 292 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide292 Lys Lys Ser Ile Gln Phe His Trp Lys Asn Ser Asn Gln Ile Lys Ile 1 510 15 Leu Gly Asn Gln Gly 20 293 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 293 Phe His Trp Lys Asn Ser AsnGln Ile Lys Ile Leu Gly Asn Gln Gly 1 5 10 15 Ser Phe Leu Thr Lys 20 29421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 294 Ser Asn Gln Ile Lys Ile Leu Gly Asn Gln Gly Ser Phe Leu ThrLys 1 5 10 15 Gly Pro Ser Lys Leu 20 295 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 295 Ile Leu Gly AsnGln Gly Ser Phe Leu Thr Lys Gly Pro Ser Lys Leu 1 5 10 15 Asn Asp ArgAla Asp 20 296 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 296 Gly Ser Phe Leu Thr Lys Gly Pro Ser Lys LeuAsn Asp Arg Ala Asp 1 5 10 15 Ser Arg Arg Ser Leu 20 297 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide297 Lys Gly Pro Ser Lys Leu Asn Asp Arg Ala Asp Ser Arg Arg Ser Leu 1 510 15 Trp Asp Gln Gly Asn 20 298 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 298 Leu Asn Asp Arg Ala Asp SerArg Arg Ser Leu Trp Asp Gln Gly Asn 1 5 10 15 Phe Pro Leu Ile Ile 20 29921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 299 Asp Ser Arg Arg Ser Leu Trp Asp Gln Gly Asn Phe Pro Leu IleIle 1 5 10 15 Lys Asn Leu Lys Ile 20 300 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 300 Leu Trp Asp GlnGly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile 1 5 10 15 Glu Asp SerAsp Thr 20 301 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 301 Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys IleGlu Asp Ser Asp Thr 1 5 10 15 Tyr Ile Cys Glu Val 20 302 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide302 Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val 1 510 15 Glu Asp Gln Lys Glu 20 303 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 303 Ile Glu Asp Ser Asp Thr TyrIle Cys Glu Val Glu Asp Gln Lys Glu 1 5 10 15 Glu Val Gln Leu Leu 20 30421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 304 Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln LeuLeu 1 5 10 15 Val Phe Gly Leu Thr 20 305 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 305 Val Glu Asp GlnLys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr 1 5 10 15 Ala Asn SerAsp Thr 20 306 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 306 Glu Glu Val Gln Leu Leu Val Phe Gly Leu ThrAla Asn Ser Asp Thr 1 5 10 15 His Leu Leu Gln Gly 20 307 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide307 Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly 1 510 15 Gln Ser Leu Thr Leu 20 308 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 308 Thr Ala Asn Ser Asp Thr HisLeu Leu Gln Gly Gln Ser Leu Thr Leu 1 5 10 15 Thr Leu Glu Ser Pro 20 30921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 309 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu SerPro 1 5 10 15 Pro Gly Ser Ser Pro 20 310 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 310 Gly Gln Ser LeuThr Leu Thr Leu Glu Ser Pro Pro Gly Ser Ser Pro 1 5 10 15 Ser Val GlnCys Arg 20 311 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 311 Leu Thr Leu Glu Ser Pro Pro Gly Ser Ser ProSer Val Gln Cys Arg 1 5 10 15 Ser Pro Arg Gly Lys 20 312 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide312 Pro Pro Gly Ser Ser Pro Ser Val Gln Cys Arg Ser Pro Arg Gly Lys 1 510 15 Asn Ile Gln Gly Gly 20 313 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 313 Pro Ser Val Gln Cys Arg SerPro Arg Gly Lys Asn Ile Gln Gly Gly 1 5 10 15 Lys Thr Leu Ser Val 20 31421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 314 Arg Ser Pro Arg Gly Lys Asn Ile Gln Gly Gly Lys Thr Leu SerVal 1 5 10 15 Ser Gln Leu Glu Leu 20 315 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 315 Lys Asn Ile GlnGly Gly Lys Thr Leu Ser Val Ser Gln Leu Glu Leu 1 5 10 15 Gln Asp SerGly Thr 20 316 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 316 Gly Lys Thr Leu Ser Val Ser Gln Leu Glu LeuGln Asp Ser Gly Thr 1 5 10 15 Trp Thr Cys Thr Val 20 317 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide317 Val Ser Gln Leu Glu Leu Gln Asp Ser Gly Thr Trp Thr Cys Thr Val 1 510 15 Leu Gln Asn Gln Lys 20 318 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 318 Leu Gln Asp Ser Gly Thr TrpThr Cys Thr Val Leu Gln Asn Gln Lys 1 5 10 15 Lys Val Glu Phe Lys 20 31921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 319 Thr Trp Thr Cys Thr Val Leu Gln Asn Gln Lys Lys Val Glu PheLys 1 5 10 15 Ile Asp Ile Val Val 20 320 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 320 Val Leu Gln AsnGln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val 1 5 10 15 Leu Ala PheGln Lys 20 321 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 321 Lys Lys Val Glu Phe Lys Ile Asp Ile Val ValLeu Ala Phe Gln Lys 1 5 10 15 Ala Ser Ser Ile Val 20 322 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide322 Lys Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val 1 510 15 Tyr Lys Lys Glu Gly 20 323 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 323 Val Leu Ala Phe Gln Lys AlaSer Ser Ile Val Tyr Lys Lys Glu Gly 1 5 10 15 Glu Gln Val Glu Phe 20 32421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 324 Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val GluPhe 1 5 10 15 Ser Phe Pro Leu Ala 20 325 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 325 Val Tyr Lys LysGlu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala 1 5 10 15 Phe Thr ValGlu Lys 20 326 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 326 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu AlaPhe Thr Val Glu Lys 1 5 10 15 Leu Thr Gly Ser Gly 20 327 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide327 Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly 1 510 15 Glu Leu Trp Trp Gln 20 328 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 328 Ala Phe Thr Val Glu Lys LeuThr Gly Ser Gly Glu Leu Trp Trp Gln 1 5 10 15 Ala Glu Arg Ala Ser 20 32921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 329 Lys Leu Thr Gly Ser Gly Glu Leu Trp Trp Gln Ala Glu Arg AlaSer 1 5 10 15 Ser Ser Lys Ser Trp 20 330 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 330 Gly Glu Leu TrpTrp Gln Ala Glu Arg Ala Ser Ser Ser Lys Ser Trp 1 5 10 15 Ile Thr PheAsp Leu 20 331 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 331 Gln Ala Glu Arg Ala Ser Ser Ser Lys Ser TrpIle Thr Phe Asp Leu 1 5 10 15 Lys Asn Lys Glu Val 20 332 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide332 Ser Ser Ser Lys Ser Trp Ile Thr Phe Asp Leu Lys Asn Lys Glu Val 1 510 15 Ser Val Lys Arg Val 20 333 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 333 Trp Ile Thr Phe Asp Leu LysAsn Lys Glu Val Ser Val Lys Arg Val 1 5 10 15 Thr Gln Asp Pro Lys 20 33421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 334 Leu Lys Asn Lys Glu Val Ser Val Lys Arg Val Thr Gln Asp ProLys 1 5 10 15 Leu Gln Met Gly Lys 20 335 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 335 Val Ser Val LysArg Val Thr Gln Asp Pro Lys Leu Gln Met Gly Lys 1 5 10 15 Lys Leu ProLeu His 20 336 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 336 Val Thr Gln Asp Pro Lys Leu Gln Met Gly LysLys Leu Pro Leu His 1 5 10 15 Leu Thr Leu Pro Gln 20 337 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide337 Lys Leu Gln Met Gly Lys Lys Leu Pro Leu His Leu Thr Leu Pro Gln 1 510 15 Ala Leu Pro Gln Tyr 20 338 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 338 Lys Lys Leu Pro Leu His LeuThr Leu Pro Gln Ala Leu Pro Gln Tyr 1 5 10 15 Ala Gly Ser Gly Asn 20 33921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 339 His Leu Thr Leu Pro Gln Ala Leu Pro Gln Tyr Ala Gly Ser GlyAsn 1 5 10 15 Leu Thr Leu Ala Leu 20 340 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 340 Gln Ala Leu ProGln Tyr Ala Gly Ser Gly Asn Leu Thr Leu Ala Leu 1 5 10 15 Glu Ala LysThr Gly 20 341 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 341 Tyr Ala Gly Ser Gly Asn Leu Thr Leu Ala LeuGlu Ala Lys Thr Gly 1 5 10 15 Lys Leu His Gln Glu 20 342 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide342 Asn Leu Thr Leu Ala Leu Glu Ala Lys Thr Gly Lys Leu His Gln Glu 1 510 15 Val Asn Leu Val Val 20 343 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 343 Leu Glu Ala Lys Thr Gly LysLeu His Gln Glu Val Asn Leu Val Val 1 5 10 15 Met Arg Ala Thr Gln 20 34421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 344 Gly Lys Leu His Gln Glu Val Asn Leu Val Val Met Arg Ala ThrGln 1 5 10 15 Leu Gln Lys Asn Leu 20 345 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 345 Glu Val Asn LeuVal Val Met Arg Ala Thr Gln Leu Gln Lys Asn Leu 1 5 10 15 Thr Cys GluVal Trp 20 346 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 346 Val Met Arg Ala Thr Gln Leu Gln Lys Asn LeuThr Cys Glu Val Trp 1 5 10 15 Gly Pro Thr Ser Pro 20 347 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide347 Gln Leu Gln Lys Asn Leu Thr Cys Glu Val Trp Gly Pro Thr Ser Pro 1 510 15 Lys Leu Met Leu Ser 20 348 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 348 Leu Thr Cys Glu Val Trp GlyPro Thr Ser Pro Lys Leu Met Leu Ser 1 5 10 15 Leu Lys Leu Glu Asn 20 34921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 349 Trp Gly Pro Thr Ser Pro Lys Leu Met Leu Ser Leu Lys Leu GluAsn 1 5 10 15 Lys Glu Ala Lys Val 20 350 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 350 Pro Lys Leu MetLeu Ser Leu Lys Leu Glu Asn Lys Glu Ala Lys Val 1 5 10 15 Ser Lys ArgGlu Lys 20 351 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 351 Ser Leu Lys Leu Glu Asn Lys Glu Ala Lys ValSer Lys Arg Glu Lys 1 5 10 15 Ala Val Trp Val Leu 20 352 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide352 Asn Lys Glu Ala Lys Val Ser Lys Arg Glu Lys Ala Val Trp Val Leu 1 510 15 Asn Pro Glu Ala Gly 20 353 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 353 Val Ser Lys Arg Glu Lys AlaVal Trp Val Leu Asn Pro Glu Ala Gly 1 5 10 15 Met Trp Gln Cys Leu 20 35421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 354 Lys Ala Val Trp Val Leu Asn Pro Glu Ala Gly Met Trp Gln CysLeu 1 5 10 15 Leu Ser Asp Ser Gly 20 355 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 355 Leu Asn Pro GluAla Gly Met Trp Gln Cys Leu Leu Ser Asp Ser Gly 1 5 10 15 Gln Val LeuLeu Glu 20 356 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 356 Gly Met Trp Gln Cys Leu Leu Ser Asp Ser GlyGln Val Leu Leu Glu 1 5 10 15 Ser Asn Ile Lys Val 20 357 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide357 Leu Leu Ser Asp Ser Gly Gln Val Leu Leu Glu Ser Asn Ile Lys Val 1 510 15 Leu Pro Thr Trp Ser 20 358 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 358 Gly Gln Val Leu Leu Glu SerAsn Ile Lys Val Leu Pro Thr Trp Ser 1 5 10 15 Thr Pro Val Gln Pro 20 35921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 359 Glu Ser Asn Ile Lys Val Leu Pro Thr Trp Ser Thr Pro Val GlnPro 1 5 10 15 Met Ala Leu Ile Val 20 360 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 360 Val Leu Pro ThrTrp Ser Thr Pro Val Gln Pro Met Ala Leu Ile Val 1 5 10 15 Leu Gly GlyVal Ala 20 361 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 361 Ser Thr Pro Val Gln Pro Met Ala Leu Ile ValLeu Gly Gly Val Ala 1 5 10 15 Gly Leu Leu Leu Phe 20 362 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide362 Pro Met Ala Leu Ile Val Leu Gly Gly Val Ala Gly Leu Leu Leu Phe 1 510 15 Ile Gly Leu Gly Ile 20 363 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 363 Val Leu Gly Gly Val Ala GlyLeu Leu Leu Phe Ile Gly Leu Gly Ile 1 5 10 15 Phe Phe Cys Val Arg 20 36421 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 364 Ala Gly Leu Leu Leu Phe Ile Gly Leu Gly Ile Phe Phe Cys ValArg 1 5 10 15 Cys Arg His Arg Arg 20 365 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 365 Phe Ile Gly LeuGly Ile Phe Phe Cys Val Arg Cys Arg His Arg Arg 1 5 10 15 Arg Gln AlaGlu Arg 20 366 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 366 Ile Phe Phe Cys Val Arg Cys Arg His Arg ArgArg Gln Ala Glu Arg 1 5 10 15 Met Ser Gln Ile Lys 20 367 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide367 Arg Cys Arg His Arg Arg Arg Gln Ala Glu Arg Met Ser Gln Ile Lys 1 510 15 Arg Leu Leu Ser Glu 20 368 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 368 Arg Arg Gln Ala Glu Arg MetSer Gln Ile Lys Arg Leu Leu Ser Glu 1 5 10 15 Lys Lys Thr Cys Gln 20 36921 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 369 Arg Met Ser Gln Ile Lys Arg Leu Leu Ser Glu Lys Lys Thr CysGln 1 5 10 15 Cys Pro His Arg Phe 20 370 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 370 Lys Arg Leu LeuSer Glu Lys Lys Thr Cys Gln Cys Pro His Arg Phe 1 5 10 15 Gln Lys ThrCys Ser 20 371 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 371 Glu Lys Lys Thr Cys Gln Cys Pro His Arg PheGln Lys Thr Cys Ser 1 5 10 15 Pro Ile 372 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 372 Met Asp Tyr GlnVal Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 373 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 373 Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr ThrSer 1 5 10 15 Glu Pro 374 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 374 Tyr Gln Val Ser Ser Pro Ile TyrAsp Ile Asn Tyr Tyr Thr Ser Glu 1 5 10 15 Pro Cys 375 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 375 Gln ValSer Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr Ser Glu Pro 1 5 10 15 CysGln 376 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 376 Val Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr SerGlu Pro Cys 1 5 10 15 Gln Lys 377 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 377 Ser Ser Pro Ile Tyr Asp IleAsn Tyr Tyr Thr Ser Glu Pro Cys Gln 1 5 10 15 Lys Ile 378 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide378 Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr Ser Glu Pro Cys Gln Lys 1 510 15 Ile Asn 379 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 379 Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr Ser GluPro Cys Gln Lys Ile 1 5 10 15 Asn Val 380 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 380 Ile Tyr Asp IleAsn Tyr Tyr Thr Ser Glu Pro Cys Gln Lys Ile Asn 1 5 10 15 Val Lys 381 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 381 Tyr Asp Ile Asn Tyr Tyr Thr Ser Glu Pro Cys Gln Lys Ile AsnVal 1 5 10 15 Lys Gln 382 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 382 Asp Ile Asn Tyr Tyr Thr Ser GluPro Cys Gln Lys Ile Asn Val Lys 1 5 10 15 Gln Ile 383 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 383 Ile AsnTyr Tyr Thr Ser Glu Pro Cys Gln Lys Ile Asn Val Lys Gln 1 5 10 15 IleAla 384 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 384 Asn Tyr Tyr Thr Ser Glu Pro Cys Gln Lys Ile Asn ValLys Gln Ile 1 5 10 15 Ala Ala 385 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 385 Tyr Tyr Thr Ser Glu Pro CysGln Lys Ile Asn Val Lys Gln Ile Ala 1 5 10 15 Ala Arg 386 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide386 Tyr Thr Ser Glu Pro Cys Gln Lys Ile Asn Val Lys Gln Ile Ala 1 5 1015 387 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 387 Thr Ser Glu Pro Cys Gln Lys Ile Asn Val Lys Gln IleAla Ala 1 5 10 15 388 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 388 Ser Glu Pro Cys Gln Lys Ile AsnVal Lys Gln Ile Ala Ala Arg 1 5 10 15 389 12 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 389 Glu Pro Cys GlnLys Ile Asn Val Lys Gln Ile Ala 1 5 10 390 12 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 390 Pro Cys Gln LysIle Asn Val Lys Gln Ile Ala Ala 1 5 10 391 12 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 391 Cys Gln Lys IleAsn Val Lys Gln Ile Ala Ala Arg 1 5 10 392 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 392 Gln Lys Ile AsnVal Lys Gln Ile Ala 1 5 393 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 393 Lys Ile Asn Val Lys Gln Ile AlaAla 1 5 394 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 394 Ile Asn Val Lys Gln Ile Ala Ala Arg 1 5 395 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide395 Met Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met 1 510 15 Gly Ser 396 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 396 Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn TyrThr Glu Glu Met Gly 1 5 10 15 Ser Gly 397 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 397 Gly Ile Ser IleTyr Thr Ser Asp Asn Tyr Thr Glu Glu Met Gly Ser 1 5 10 15 Gly Asp 398 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 398 Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met Gly SerGly 1 5 10 15 Asp Tyr 399 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 399 Ser Ile Tyr Thr Ser Asp Asn TyrThr Glu Glu Met Gly Ser Gly Asp 1 5 10 15 Tyr Asp 400 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 400 Ile TyrThr Ser Asp Asn Tyr Thr Glu Glu Met Gly Ser Gly Asp Tyr 1 5 10 15 AspSer 401 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 401 Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met Gly Ser GlyAsp Tyr Asp 1 5 10 15 Ser Met 402 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 402 Thr Ser Asp Asn Tyr Thr GluGlu Met Gly Ser Gly Asp Tyr Asp Ser 1 5 10 15 Met Lys 403 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide403 Ser Asp Asn Tyr Thr Glu Glu Met Gly Ser Gly Asp Tyr Asp Ser Met 1 510 15 Lys Glu 404 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 404 Asp Asn Tyr Thr Glu Glu Met Gly Ser Gly AspTyr Asp Ser Met Lys 1 5 10 15 Glu Pro 405 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 405 Asn Tyr Thr GluGlu Met Gly Ser Gly Asp Tyr Asp Ser Met Lys Glu 1 5 10 15 Pro Cys 406 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 406 Tyr Thr Glu Glu Met Gly Ser Gly Asp Tyr Asp Ser Met Lys GluPro 1 5 10 15 Cys Phe 407 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 407 Thr Glu Glu Met Gly Ser Gly AspTyr Asp Ser Met Lys Glu Pro Cys 1 5 10 15 Phe Arg 408 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 408 Glu GluMet Gly Ser Gly Asp Tyr Asp Ser Met Lys Glu Pro Cys Phe 1 5 10 15 ArgGlu 409 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 409 Glu Met Gly Ser Gly Asp Tyr Asp Ser Met Lys Glu ProCys Phe Arg 1 5 10 15 Glu Glu 410 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 410 Met Gly Ser Gly Asp Tyr AspSer Met Lys Glu Pro Cys Phe Arg Glu 1 5 10 15 Glu Asn 411 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide411 Gly Ser Gly Asp Tyr Asp Ser Met Lys Glu Pro Cys Phe Arg Glu Glu 1 510 15 Asn Ala 412 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 412 Ser Gly Asp Tyr Asp Ser Met Lys Glu Pro CysPhe Arg Glu Glu Asn 1 5 10 15 Ala Asn 413 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 413 Gly Asp Tyr AspSer Met Lys Glu Pro Cys Phe Arg Glu Glu Asn Ala 1 5 10 15 Asn Phe 414 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 414 Asp Tyr Asp Ser Met Lys Glu Pro Cys Phe Arg Glu Glu Asn AlaAsn 1 5 10 15 Phe Asn 415 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 415 Tyr Asp Ser Met Lys Glu Pro CysPhe Arg Glu Glu Asn Ala Asn Phe 1 5 10 15 Asn Lys 416 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 416 Asp SerMet Lys Glu Pro Cys Phe Arg Glu Glu Asn Ala Asn Phe Asn 1 5 10 15 LysIle 417 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 417 Ser Met Lys Glu Pro Cys Phe Arg Glu Glu Asn Ala AsnPhe Asn 1 5 10 15 418 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 418 Met Lys Glu Pro Cys Phe Arg GluGlu Asn Ala Asn Phe Asn Lys 1 5 10 15 419 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 419 Lys Glu Pro CysPhe Arg Glu Glu Asn Ala Asn Phe Asn Lys Ile 1 5 10 15 420 12 PRTArtificial Sequence Description of Artificial Sequence binding peptide420 Glu Pro Cys Phe Arg Glu Glu Asn Ala Asn Phe Asn 1 5 10 421 12 PRTArtificial Sequence Description of Artificial Sequence binding peptide421 Pro Cys Phe Arg Glu Glu Asn Ala Asn Phe Asn Lys 1 5 10 422 12 PRTArtificial Sequence Description of Artificial Sequence binding peptide422 Cys Phe Arg Glu Glu Asn Ala Asn Phe Asn Lys Ile 1 5 10 423 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide423 Arg Glu Glu Asn Ala Asn Phe Asn Lys 1 5 424 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 424 Met AlaGlu His Asp Tyr His Glu Asp Tyr Gly Phe Ser Ser Phe Asn 1 5 10 15 AspSer 425 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 425 Ala Glu His Asp Tyr His Glu Asp Tyr Gly Phe Ser SerPhe Asn Asp 1 5 10 15 Ser Ser 426 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 426 Glu His Asp Tyr His Glu AspTyr Gly Phe Ser Ser Phe Asn Asp Ser 1 5 10 15 Ser Gln 427 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide427 His Asp Tyr His Glu Asp Tyr Gly Phe Ser Ser Phe Asn Asp Ser Ser 1 510 15 Gln Glu 428 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 428 Asp Tyr His Glu Asp Tyr Gly Phe Ser Ser PheAsn Asp Ser Ser Gln 1 5 10 15 Glu Glu 429 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 429 Tyr His Glu AspTyr Gly Phe Ser Ser Phe Asn Asp Ser Ser Gln Glu 1 5 10 15 Glu His 430 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 430 His Glu Asp Tyr Gly Phe Ser Ser Phe Asn Asp Ser Ser Gln GluGlu 1 5 10 15 His Gln 431 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 431 Glu Asp Tyr Gly Phe Ser Ser PheAsn Asp Ser Ser Gln Glu Glu His 1 5 10 15 Gln Ala 432 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 432 Asp TyrGly Phe Ser Ser Phe Asn Asp Ser Ser Gln Glu Glu His Gln 1 5 10 15 AlaPhe 433 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 433 Tyr Gly Phe Ser Ser Phe Asn Asp Ser Ser Gln Glu GluHis Gln Ala 1 5 10 15 Phe Leu 434 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 434 Gly Phe Ser Ser Phe Asn AspSer Ser Gln Glu Glu His Gln Ala Phe 1 5 10 15 Leu Gln 435 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide435 Phe Ser Ser Phe Asn Asp Ser Ser Gln Glu Glu His Gln Ala Phe Leu 1 510 15 Gln Phe 436 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 436 Ser Ser Phe Asn Asp Ser Ser Gln Glu Glu HisGln Ala Phe Leu Gln 1 5 10 15 Phe Ser 437 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 437 Ser Phe Asn AspSer Ser Gln Glu Glu His Gln Ala Phe Leu Gln Phe 1 5 10 15 Ser Lys 438 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 438 Phe Asn Asp Ser Ser Gln Glu Glu His Gln Ala Phe Leu Gln PheSer 1 5 10 15 Lys Val 439 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 439 Asn Asp Ser Ser Gln Glu Glu HisGln Ala Phe Leu Gln Phe Ser 1 5 10 15 440 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 440 Asp Ser Ser GlnGlu Glu His Gln Ala Phe Leu Gln Phe Ser Lys 1 5 10 15 441 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide441 Ser Ser Gln Glu Glu His Gln Ala Phe Leu Gln Phe Ser Lys Val 1 5 1015 442 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 442 Ser Gln Glu Glu His Gln Ala Phe Leu Gln Phe Ser 1 510 443 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 443 Gln Glu Glu His Gln Ala Phe Leu Gln Phe Ser Lys 1 510 444 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 444 Glu Glu His Gln Ala Phe Leu Gln Phe Ser Lys Val 1 510 445 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 445 Glu His Gln Ala Phe Leu Gln Phe Ser 1 5 446 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide446 His Gln Ala Phe Leu Gln Phe Ser Lys 1 5 447 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 447 Gln AlaPhe Leu Gln Phe Ser Lys Val 1 5 448 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 448 Met Asp Tyr GlnVal Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 449 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 449 Ala Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ile Asn Tyr TyrThr 1 5 10 15 Ser Glu 450 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 450 Met Ala Tyr Gln Val Ser Ser ProIle Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 451 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 451 Met AspAla Gln Val Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 SerGlu 452 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 452 Met Asp Tyr Ala Val Ser Ser Pro Ile Tyr Asp Ile AsnTyr Tyr Thr 1 5 10 15 Ser Glu 453 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 453 Met Asp Tyr Gln Ala Ser SerPro Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 454 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide454 Met Asp Tyr Gln Val Ala Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 510 15 Ser Glu 455 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 455 Met Asp Tyr Gln Val Ser Ala Pro Ile Tyr AspIle Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 456 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 456 Met Asp Tyr GlnVal Ser Ser Ala Ile Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 457 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 457 Met Asp Tyr Gln Val Ser Ser Pro Ala Tyr Asp Ile Asn Tyr TyrThr 1 5 10 15 Ser Glu 458 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 458 Met Asp Tyr Gln Val Ser Ser ProIle Ala Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Glu 459 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 459 Met AspTyr Gln Val Ser Ser Pro Ile Tyr Ala Ile Asn Tyr Tyr Thr 1 5 10 15 SerGlu 460 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 460 Met Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ala AsnTyr Tyr Thr 1 5 10 15 Ser Glu 461 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 461 Met Asp Tyr Gln Val Ser SerPro Ile Tyr Asp Ile Ala Tyr Tyr Thr 1 5 10 15 Ser Glu 462 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide462 Met Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ile Asn Ala Tyr Thr 1 510 15 Ser Glu 463 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 463 Met Asp Tyr Gln Val Ser Ser Pro Ile Tyr AspIle Asn Tyr Ala Thr 1 5 10 15 Ser Glu 464 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 464 Met Asp Tyr GlnVal Ser Ser Pro Ile Tyr Asp Ile Asn Tyr Tyr Ala 1 5 10 15 Ser Glu 465 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 465 Met Asp Tyr Gln Val Ser Ser Pro Ile Tyr Asp Ile Asn Tyr TyrThr 1 5 10 15 Ala Glu 466 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 466 Met Asp Tyr Gln Val Ser Ser ProIle Tyr Asp Ile Asn Tyr Tyr Thr 1 5 10 15 Ser Ala 467 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 467 Met GluGly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met 1 5 10 15 GlySer 468 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 468 Ala Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr ThrGlu Glu Met 1 5 10 15 Gly Ser 469 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 469 Met Ala Gly Ile Ser Ile TyrThr Ser Asp Asn Tyr Thr Glu Glu Met 1 5 10 15 Gly Ser 470 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide470 Met Glu Ala Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met 1 510 15 Gly Ser 471 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 471 Met Glu Gly Ala Ser Ile Tyr Thr Ser Asp AsnTyr Thr Glu Glu Met 1 5 10 15 Gly Ser 472 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 472 Met Glu Gly IleAla Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Met 1 5 10 15 Gly Ser 473 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 473 Met Glu Gly Ile Ser Ala Tyr Thr Ser Asp Asn Tyr Thr Glu GluMet 1 5 10 15 Gly Ser 474 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 474 Met Glu Gly Ile Ser Ile Ala ThrSer Asp Asn Tyr Thr Glu Glu Met 1 5 10 15 Gly Ser 475 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 475 Met GluGly Ile Ser Ile Tyr Ala Ser Asp Asn Tyr Thr Glu Glu Met 1 5 10 15 GlySer 476 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 476 Met Glu Gly Ile Ser Ile Tyr Thr Ala Asp Asn Tyr ThrGlu Glu Met 1 5 10 15 Gly Ser 477 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 477 Met Glu Gly Ile Ser Ile TyrThr Ser Ala Asn Tyr Thr Glu Glu Met 1 5 10 15 Gly Ser 478 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide478 Met Glu Gly Ile Ser Ile Tyr Thr Ser Asp Ala Tyr Thr Glu Glu Met 1 510 15 Gly Ser 479 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 479 Met Glu Gly Ile Ser Ile Tyr Thr Ser Asp AsnAla Thr Glu Glu Met 1 5 10 15 Gly Ser 480 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 480 Met Glu Gly IleSer Ile Tyr Thr Ser Asp Asn Tyr Ala Glu Glu Met 1 5 10 15 Gly Ser 481 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 481 Met Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Ala GluMet 1 5 10 15 Gly Ser 482 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 482 Met Glu Gly Ile Ser Ile Tyr ThrSer Asp Asn Tyr Thr Glu Ala Met 1 5 10 15 Gly Ser 483 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 483 Met GluGly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr Thr Glu Glu Ala 1 5 10 15 GlySer 484 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 484 Met Glu Gly Ile Ser Ile Tyr Thr Ser Asp Asn Tyr ThrGlu Glu Met 1 5 10 15 Ala Ser 485 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 485 Met Glu Gly Ile Ser Ile TyrThr Ser Asp Asn Tyr Thr Glu Glu Met 1 5 10 15 Gly Ala 486 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide486 Glu Glu His Gln Ala Phe Leu Gln Phe Ser Lys Val Phe Leu Pro Cys 1 510 15 Met Tyr 487 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 487 Ala Glu His Gln Ala Phe Leu Gln Phe Ser LysVal Phe Leu Pro Cys 1 5 10 15 Met Tyr 488 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 488 Glu Ala His GlnAla Phe Leu Gln Phe Ser Lys Val Phe Leu Pro Cys 1 5 10 15 Met Tyr 489 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 489 Glu Glu Ala Gln Ala Phe Leu Gln Phe Ser Lys Val Phe Leu ProCys 1 5 10 15 Met Tyr 490 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 490 Glu Glu His Ala Ala Phe Leu GlnPhe Ser Lys Val Phe Leu Pro Cys 1 5 10 15 Met Tyr 491 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 491 Glu GluHis Gln Ala Phe Leu Gln Phe Ser Lys Val Phe Leu Pro Cys 1 5 10 15 MetTyr 492 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 492 Glu Glu His Gln Ala Ala Leu Gln Phe Ser Lys Val PheLeu Pro Cys 1 5 10 15 Met Tyr 493 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 493 Glu Glu His Gln Ala Phe AlaGln Phe Ser Lys Val Phe Leu Pro Cys 1 5 10 15 Met Tyr 494 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide494 Glu Glu His Gln Ala Phe Leu Ala Phe Ser Lys Val Phe Leu Pro Cys 1 510 15 Met Tyr 495 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 495 Glu Glu His Gln Ala Phe Leu Gln Ala Ser LysVal Phe Leu Pro Cys 1 5 10 15 Met Tyr 496 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 496 Glu Glu His GlnAla Phe Leu Gln Phe Ala Lys Val Phe Leu Pro Cys 1 5 10 15 Met Tyr 497 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 497 Glu Glu His Gln Ala Phe Leu Gln Phe Ser Ala Val Phe Leu ProCys 1 5 10 15 Met Tyr 498 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 498 Glu Glu His Gln Ala Phe Leu GlnPhe Ser Lys Ala Phe Leu Pro Cys 1 5 10 15 Met Tyr 499 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 499 Glu GluHis Gln Ala Phe Leu Gln Phe Ser Lys Val Ala Leu Pro Cys 1 5 10 15 MetTyr 500 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 500 Glu Glu His Gln Ala Phe Leu Gln Phe Ser Lys Val PheAla Pro Cys 1 5 10 15 Met Tyr 501 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 501 Glu Glu His Gln Ala Phe LeuGln Phe Ser Lys Val Phe Leu Ala Cys 1 5 10 15 Met Tyr 502 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide502 Glu Glu His Gln Ala Phe Leu Gln Phe Ser Lys Val Phe Leu Pro Ala 1 510 15 Met Tyr 503 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 503 Glu Glu His Gln Ala Phe Leu Gln Phe Ser LysVal Phe Leu Pro Cys 1 5 10 15 Ala Tyr 504 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 504 Glu Glu His GlnAla Phe Leu Gln Phe Ser Lys Val Phe Leu Pro Cys 1 5 10 15 Met Ala 505 9PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 505 Asp Thr Tyr Ile Cys Glu Val Glu Asp 1 5 506 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 506 Lys GluGlu Val Gln Leu Leu Val Phe 1 5 507 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 507 Glu Glu Val GlnLeu Leu Val Phe Gly 1 5 508 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 508 Glu Val Gln Leu Leu Val Phe GlyLeu 1 5 509 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 509 Glu Gln Val Glu Phe Ser Phe Pro Leu 1 5 510 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide510 Gln Val Glu Phe Ser Phe Pro Leu Ala 1 5 511 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 511 Val GluPhe Ser Phe Pro Leu Ala Phe 1 5 512 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 512 Cys Glu Val GluAsp Gln Lys Glu Glu Val Gln Leu Leu Val Phe 1 5 10 15 513 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide513 Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly 1 5 1015 514 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 514 Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val PheGly Leu 1 5 10 15 515 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 515 Glu Asp Gln Lys Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr 1 5 10 15 516 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 516 Asp Gln Lys GluGlu Val Gln Leu Leu Val Phe Gly Leu Thr Ala 1 5 10 15 517 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide517 Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn 1 5 1015 518 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 518 Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr AlaAsn Ser 1 5 10 15 519 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 519 Glu Glu Val Gln Leu Leu Val PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 520 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 520 Glu Val Gln LeuLeu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr 1 5 10 15 521 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide521 Asp Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 5 1015 522 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 522 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 523 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 523 His Leu Leu Gln Gly Gln Ser LeuThr Leu Thr Leu Glu Ser Pro 1 5 10 15 524 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 524 Lys Lys Glu GlyGlu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe 1 5 10 15 525 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide525 Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr 1 5 1015 526 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 526 Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala PheThr Val 1 5 10 15 527 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 527 Gly Glu Gln Val Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 528 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 528 Glu Gln Val GluPhe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys 1 5 10 15 529 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide529 Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu 1 5 1015 530 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 530 Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu 1 510 531 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 531 Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe 1 510 532 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 532 Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly 1 510 533 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 533 Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu 1 510 534 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 534 Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr 1 510 535 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 535 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala 1 510 536 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 536 Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn 1 510 537 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 537 Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 510 538 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 538 Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala 1 510 539 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 539 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe 1 510 540 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 540 Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr 1 510 541 12 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 541 Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val 1 510 542 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 542 Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu GluVal Gln Leu 1 5 10 15 Leu Val 543 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 543 Thr Tyr Ile Cys Glu Val GluAsp Gln Lys Glu Glu Val Gln Leu Leu 1 5 10 15 Val Phe 544 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide544 Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val 1 510 15 Phe Gly 545 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 545 Ile Cys Glu Val Glu Asp Gln Lys Glu Glu ValGln Leu Leu Val Phe 1 5 10 15 Gly Leu 546 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 546 Cys Glu Val GluAsp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly 1 5 10 15 Leu Thr 547 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 547 Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe GlyLeu 1 5 10 15 Thr Ala 548 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 548 Val Glu Asp Gln Lys Glu Glu ValGln Leu Leu Val Phe Gly Leu Thr 1 5 10 15 Ala Asn 549 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 549 Glu AspGln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala 1 5 10 15 AsnSer 550 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 550 Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly LeuThr Ala Asn 1 5 10 15 Ser Asp 551 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 551 Gln Lys Glu Glu Val Gln LeuLeu Val Phe Gly Leu Thr Ala Asn Ser 1 5 10 15 Asp Thr 552 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide552 Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr 1 510 15 Leu Glu 553 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 553 Asn Ser Asp Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu 1 5 10 15 Glu Ser 554 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 554 Ser Asp Thr HisLeu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 5 10 15 Ser Pro 555 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 555 Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe ProLeu 1 5 10 15 Ala Phe 556 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 556 Val Tyr Lys Lys Glu Gly Glu GlnVal Glu Phe Ser Phe Pro Leu Ala 1 5 10 15 Phe Thr 557 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 557 Tyr LysLys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe 1 5 10 15 ThrVal 558 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 558 Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro LeuAla Phe Thr 1 5 10 15 Val Glu 559 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 559 Lys Glu Gly Glu Gln Val GluPhe Ser Phe Pro Leu Ala Phe Thr Val 1 5 10 15 Glu Lys 560 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide560 Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 510 15 Lys Leu 561 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 561 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu AlaPhe Thr Val Glu Lys 1 5 10 15 Leu Thr 562 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 562 Gly Asn Phe ProLeu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp 1 5 10 15 Thr Tyr IleCys Glu 20 563 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 563 Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys IleGlu Asp Ser Asp Thr 1 5 10 15 Tyr Ile Cys Glu Val 20 564 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide564 Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr 1 510 15 Ile Cys Glu Val Glu 20 565 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 565 Pro Leu Ile Ile Lys Asn LeuLys Ile Glu Asp Ser Asp Thr Tyr Ile 1 5 10 15 Cys Glu Val Glu Asp 20 56621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 566 Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr IleCys 1 5 10 15 Glu Val Glu Asp Gln 20 567 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 567 Ile Ile Lys AsnLeu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu 1 5 10 15 Val Glu AspGln Lys 20 568 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 568 Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp ThrTyr Ile Cys Glu Val 1 5 10 15 Glu Asp Gln Lys Glu 20 569 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide569 Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu 1 510 15 Asp Gln Lys Glu Glu 20 570 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 570 Leu Lys Ile Glu Asp Ser AspThr Tyr Ile Cys Glu Val Glu Asp Gln 1 5 10 15 Lys Glu Glu Val Gln 20 57121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 571 Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp GlnLys 1 5 10 15 Glu Glu Val Gln Leu 20 572 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 572 Ile Glu Asp SerAsp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu 1 5 10 15 Glu Val GlnLeu Leu 20 573 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 573 Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val GluAsp Gln Lys Glu Glu 1 5 10 15 Val Gln Leu Leu Val 20 574 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide574 Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val 1 510 15 Gln Leu Leu Val Phe 20 575 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 575 Ser Asp Thr Tyr Ile Cys GluVal Glu Asp Gln Lys Glu Glu Val Gln 1 5 10 15 Leu Leu Val Phe Gly 20 57621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 576 Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val GlnLeu 1 5 10 15 Leu Val Phe Gly Leu 20 577 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 577 Thr Tyr Ile CysGlu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu 1 5 10 15 Val Phe GlyLeu Thr 20 578 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 578 Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu GluVal Gln Leu Leu Val 1 5 10 15 Phe Gly Leu Thr Ala 20 579 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide579 Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe 1 510 15 Gly Leu Thr Ala Asn 20 580 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 580 Cys Glu Val Glu Asp Gln LysGlu Glu Val Gln Leu Leu Val Phe Gly 1 5 10 15 Leu Thr Ala Asn Ser 20 58121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 581 Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly GlnSer 1 5 10 15 Leu Thr Leu Thr Leu 20 582 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 582 Gly Leu Thr AlaAsn Ser Asp Thr His Leu Leu Gln Gly Gln Ser Leu 1 5 10 15 Thr Leu ThrLeu Glu 20 583 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 583 Leu Thr Ala Asn Ser Asp Thr His Leu Leu GlnGly Gln Ser Leu Thr 1 5 10 15 Leu Thr Leu Glu Ser 20 584 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide584 Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu 1 510 15 Thr Leu Glu Ser Pro 20 585 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 585 Phe Gln Lys Ala Ser Ser IleVal Tyr Lys Lys Glu Gly Glu Gln Val 1 5 10 15 Glu Phe Ser Phe Pro 20 58621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 586 Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln ValGlu 1 5 10 15 Phe Ser Phe Pro Leu 20 587 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 587 Lys Ala Ser SerIle Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe 1 5 10 15 Ser Phe ProLeu Ala 20 588 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 588 Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly GluGln Val Glu Phe Ser 1 5 10 15 Phe Pro Leu Ala Phe 20 589 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide589 Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe 1 510 15 Pro Leu Ala Phe Thr 20 590 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 590 Ser Ile Val Tyr Lys Lys GluGly Glu Gln Val Glu Phe Ser Phe Pro 1 5 10 15 Leu Ala Phe Thr Val 20 59121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 591 Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe ProLeu 1 5 10 15 Ala Phe Thr Val Glu 20 592 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 592 Phe Ser Phe ProLeu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly 1 5 10 15 Glu Leu TrpTrp Gln 20 593 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 593 Ser Phe Pro Leu Ala Phe Thr Val Glu Lys LeuThr Gly Ser Gly Glu 1 5 10 15 Leu Trp Trp Gln Ala 20 594 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide594 Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu Leu 1 510 15 Trp Trp Gln Ala Glu 20 595 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 595 Pro Leu Ala Phe Thr Val GluLys Leu Thr Gly Ser Gly Glu Leu Trp 1 5 10 15 Trp Gln Ala Glu Arg 20 59621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 596 Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu Leu TrpTrp 1 5 10 15 Gln Ala Glu Arg Ala 20 597 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 597 Leu Trp Asp GlnGly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile 1 5 10 15 Glu Asp SerAsp Thr 20 598 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 598 Trp Asp Gln Gly Asn Phe Pro Leu Ile Ile LysAsn Leu Lys Ile Glu 1 5 10 15 Asp Ser Asp Thr Tyr 20 599 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide599 Asp Gln Gly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp 1 510 15 Ser Asp Thr Tyr Ile 20 600 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 600 Gln Gly Asn Phe Pro Leu IleIle Lys Asn Leu Lys Ile Glu Asp Ser 1 5 10 15 Asp Thr Tyr Ile Cys 20 60121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 601 Gly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp SerAsp 1 5 10 15 Thr Tyr Ile Cys Glu 20 602 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 602 Asn Phe Pro LeuIle Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr 1 5 10 15 Tyr Ile CysGlu Val 20 603 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 603 Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile GluAsp Ser Asp Thr Tyr 1 5 10 15 Ile Cys Glu Val Glu 20 604 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide604 Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile 1 510 15 Cys Glu Val Glu Asp 20 605 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 605 Leu Ile Ile Lys Asn Leu LysIle Glu Asp Ser Asp Thr Tyr Ile Cys 1 5 10 15 Glu Val Glu Asp Gln 20 60621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 606 Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile CysGlu 1 5 10 15 Val Glu Asp Gln Lys 20 607 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 607 Ile Lys Asn LeuLys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val 1 5 10 15 Glu Asp GlnLys Glu 20 608 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 608 Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr TyrIle Cys Glu Val Glu 1 5 10 15 Asp Gln Lys Glu Glu 20 609 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide609 Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp 1 510 15 Gln Lys Glu Glu Val 20 610 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 610 Leu Lys Ile Glu Asp Ser AspThr Tyr Ile Cys Glu Val Glu Asp Gln 1 5 10 15 Lys Glu Glu Val Gln 20 61121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 611 Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp GlnLys 1 5 10 15 Glu Glu Val Gln Leu 20 612 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 612 Ile Glu Asp SerAsp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu 1 5 10 15 Glu Val GlnLeu Leu 20 613 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 613 Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val GluAsp Gln Lys Glu Glu 1 5 10 15 Val Gln Leu Leu Val 20 614 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide614 Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val 1 510 15 Gln Leu Leu Val Phe 20 615 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 615 Ser Asp Thr Tyr Ile Cys GluVal Glu Asp Gln Lys Glu Glu Val Gln 1 5 10 15 Leu Leu Val Phe Gly 20 61621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 616 Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val GlnLeu 1 5 10 15 Leu Val Phe Gly Leu 20 617 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 617 Thr Tyr Ile CysGlu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu 1 5 10 15 Val Phe GlyLeu Thr 20 618 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 618 Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu GluVal Gln Leu Leu Val 1 5 10 15 Phe Gly Leu Thr Ala 20 619 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide619 Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe 1 510 15 Gly Leu Thr Ala Asn 20 620 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 620 Cys Glu Val Glu Asp Gln LysGlu Glu Val Gln Leu Leu Val Phe Gly 1 5 10 15 Leu Thr Ala Asn Ser 20 62121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 621 Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe GlyLeu 1 5 10 15 Thr Ala Asn Ser Asp 20 622 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 622 Val Glu Asp GlnLys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr 1 5 10 15 Ala Asn SerAsp Thr 20 623 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 623 Glu Asp Gln Lys Glu Glu Val Gln Leu Leu ValPhe Gly Leu Thr Ala 1 5 10 15 Asn Ser Asp Thr His 20 624 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide624 Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn 1 510 15 Ser Asp Thr His Leu 20 625 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 625 Gln Lys Glu Glu Val Gln LeuLeu Val Phe Gly Leu Thr Ala Asn Ser 1 5 10 15 Asp Thr His Leu Leu 20 62621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 626 Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn SerAsp 1 5 10 15 Thr His Leu Leu Gln 20 627 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 627 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr 1 5 10 15 His Leu LeuGln Gly 20 628 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 628 Glu Val Gln Leu Leu Val Phe Gly Leu Thr AlaAsn Ser Asp Thr His 1 5 10 15 Leu Leu Gln Gly Gln 20 629 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide629 Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu 1 510 15 Leu Gln Gly Gln Ser 20 630 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 630 Gln Leu Leu Val Phe Gly LeuThr Ala Asn Ser Asp Thr His Leu Leu 1 5 10 15 Gln Gly Gln Ser Leu 20 63121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 631 Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu LeuGln 1 5 10 15 Gly Gln Ser Leu Thr 20 632 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 632 Leu Val Phe GlyLeu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly 1 5 10 15 Gln Ser LeuThr Leu 20 633 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 633 Val Phe Gly Leu Thr Ala Asn Ser Asp Thr HisLeu Leu Gln Gly Gln 1 5 10 15 Ser Leu Thr Leu Thr 20 634 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide634 Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser 1 510 15 Leu Thr Leu Thr Leu 20 635 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 635 Gly Leu Thr Ala Asn Ser AspThr His Leu Leu Gln Gly Gln Ser Leu 1 5 10 15 Thr Leu Thr Leu Glu 20 63621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 636 Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser LeuThr 1 5 10 15 Leu Thr Leu Glu Ser 20 637 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 637 Thr Ala Asn SerAsp Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu 1 5 10 15 Thr Leu GluSer Pro 20 638 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 638 Thr Trp Thr Cys Thr Val Leu Gln Asn Gln LysLys Val Glu Phe Lys 1 5 10 15 Ile Asp Ile Val Val 20 639 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide639 Trp Thr Cys Thr Val Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile 1 510 15 Asp Ile Val Val Leu 20 640 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 640 Thr Cys Thr Val Leu Gln AsnGln Lys Lys Val Glu Phe Lys Ile Asp 1 5 10 15 Ile Val Val Leu Ala 20 64121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 641 Cys Thr Val Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile AspIle 1 5 10 15 Val Val Leu Ala Phe 20 642 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 642 Thr Val Leu GlnAsn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val 1 5 10 15 Val Leu AlaPhe Gln 20 643 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 643 Val Leu Gln Asn Gln Lys Lys Val Glu Phe LysIle Asp Ile Val Val 1 5 10 15 Leu Ala Phe Gln Lys 20 644 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide644 Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val Leu 1 510 15 Ala Phe Gln Lys Ala 20 645 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 645 Gln Asn Gln Lys Lys Val GluPhe Lys Ile Asp Ile Val Val Leu Ala 1 5 10 15 Phe Gln Lys Ala Ser 20 64621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 646 Asn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val Leu AlaPhe 1 5 10 15 Gln Lys Ala Ser Ser 20 647 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 647 Gln Lys Lys ValGlu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln 1 5 10 15 Lys Ala SerSer Ile 20 648 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 648 Lys Lys Val Glu Phe Lys Ile Asp Ile Val ValLeu Ala Phe Gln Lys 1 5 10 15 Ala Ser Ser Ile Val 20 649 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide649 Lys Val Glu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala 1 510 15 Ser Ser Ile Val Tyr 20 650 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 650 Val Glu Phe Lys Ile Asp IleVal Val Leu Ala Phe Gln Lys Ala Ser 1 5 10 15 Ser Ile Val Tyr Lys 20 65121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 651 Glu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala SerSer 1 5 10 15 Ile Val Tyr Lys Lys 20 652 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 652 Phe Lys Ile AspIle Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile 1 5 10 15 Val Tyr LysLys Glu 20 653 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 653 Lys Ile Asp Ile Val Val Leu Ala Phe Gln LysAla Ser Ser Ile Val 1 5 10 15 Tyr Lys Lys Glu Gly 20 654 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide654 Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr 1 510 15 Lys Lys Glu Gly Glu 20 655 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 655 Asp Ile Val Val Leu Ala PheGln Lys Ala Ser Ser Ile Val Tyr Lys 1 5 10 15 Lys Glu Gly Glu Gln 20 65621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 656 Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr LysLys 1 5 10 15 Glu Gly Glu Gln Val 20 657 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 657 Val Val Leu AlaPhe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu 1 5 10 15 Gly Glu GlnVal Glu 20 658 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 658 Val Leu Ala Phe Gln Lys Ala Ser Ser Ile ValTyr Lys Lys Glu Gly 1 5 10 15 Glu Gln Val Glu Phe 20 659 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide659 Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu 1 510 15 Gln Val Glu Phe Ser 20 660 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 660 Ala Phe Gln Lys Ala Ser SerIle Val Tyr Lys Lys Glu Gly Glu Gln 1 5 10 15 Val Glu Phe Ser Phe 20 66121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 661 Phe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu GlnVal 1 5 10 15 Glu Phe Ser Phe Pro 20 662 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 662 Gln Lys Ala SerSer Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu 1 5 10 15 Phe Ser PhePro Leu 20 663 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 663 Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu GlyGlu Gln Val Glu Phe 1 5 10 15 Ser Phe Pro Leu Ala 20 664 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide664 Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser 1 510 15 Phe Pro Leu Ala Phe 20 665 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 665 Ser Ser Ile Val Tyr Lys LysGlu Gly Glu Gln Val Glu Phe Ser Phe 1 5 10 15 Pro Leu Ala Phe Thr 20 66621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 666 Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser PhePro 1 5 10 15 Leu Ala Phe Thr Val 20 667 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 667 Ile Val Tyr LysLys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu 1 5 10 15 Ala Phe ThrVal Glu 20 668 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 668 Val Tyr Lys Lys Glu Gly Glu Gln Val Glu PheSer Phe Pro Leu Ala 1 5 10 15 Phe Thr Val Glu Lys 20 669 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide669 Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe 1 510 15 Thr Val Glu Lys Leu 20 670 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 670 Lys Lys Glu Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Phe Thr 1 5 10 15 Val Glu Lys Leu Thr 20 67121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 671 Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrVal 1 5 10 15 Glu Lys Leu Thr Gly 20 672 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 672 Glu Gly Glu GlnVal Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 Lys Leu ThrGly Ser 20 673 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 673 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu AlaPhe Thr Val Glu Lys 1 5 10 15 Leu Thr Gly Ser Gly 20 674 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide674 Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu 1 510 15 Thr Gly Ser Gly Glu 20 675 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 675 Gln Val Glu Phe Ser Phe ProLeu Ala Phe Thr Val Glu Lys Leu Thr 1 5 10 15 Gly Ser Gly Glu Leu 20 67621 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 676 Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu ThrGly 1 5 10 15 Ser Gly Glu Leu Trp 20 677 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 677 Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser 1 5 10 15 Gly Glu LeuTrp Trp 20 678 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 678 Phe Ser Phe Pro Leu Ala Phe Thr Val Glu LysLeu Thr Gly Ser Gly 1 5 10 15 Glu Leu Trp Trp Gln 20 679 21 PRTArtificial Sequence Description of Artificial Sequence binding peptide679 Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu 1 510 15 Leu Trp Trp Gln Ala 20 680 21 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 680 Phe Pro Leu Ala Phe Thr ValGlu Lys Leu Thr Gly Ser Gly Glu Leu 1 5 10 15 Trp Trp Gln Ala Glu 20 68121 PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 681 Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu LeuTrp 1 5 10 15 Trp Gln Ala Glu Arg 20 682 21 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 682 Leu Ala Phe ThrVal Glu Lys Leu Thr Gly Ser Gly Glu Leu Trp Trp 1 5 10 15 Gln Ala GluArg Ala 20 683 21 PRT Artificial Sequence Description of ArtificialSequence binding peptide 683 Ala Phe Thr Val Glu Lys Leu Thr Gly Ser GlyGlu Leu Trp Trp Gln 1 5 10 15 Ala Glu Arg Ala Ser 20 684 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide684 Leu Trp Asp Gln Gly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys 1 5 1015 685 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 685 Trp Asp Gln Gly Asn Phe Pro Leu Ile Ile Lys Asn LeuLys Ile 1 5 10 15 686 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 686 Asp Gln Gly Asn Phe Pro Leu IleIle Lys Asn Leu Lys Ile Glu 1 5 10 15 687 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 687 Gln Gly Asn PhePro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp 1 5 10 15 688 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide688 Gly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser 1 5 1015 689 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 689 Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu AspSer Asp 1 5 10 15 690 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 690 Phe Pro Leu Ile Ile Lys Asn LeuLys Ile Glu Asp Ser Asp Thr 1 5 10 15 691 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 691 Pro Leu Ile IleLys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr 1 5 10 15 692 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide692 Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile 1 5 1015 693 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 693 Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr TyrIle Cys 1 5 10 15 694 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 694 Ile Lys Asn Leu Lys Ile Glu AspSer Asp Thr Tyr Ile Cys Glu 1 5 10 15 695 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 695 Lys Asn Leu LysIle Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val 1 5 10 15 696 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide696 Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu 1 5 1015 697 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 697 Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu ValGlu Asp 1 5 10 15 698 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 698 Lys Ile Glu Asp Ser Asp Thr TyrIle Cys Glu Val Glu Asp Gln 1 5 10 15 699 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 699 Ile Glu Asp SerAsp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys 1 5 10 15 700 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide700 Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu 1 5 1015 701 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 701 Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln LysGlu Glu 1 5 10 15 702 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 702 Ser Asp Thr Tyr Ile Cys Glu ValGlu Asp Gln Lys Glu Glu Val 1 5 10 15 703 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 703 Asp Thr Tyr IleCys Glu Val Glu Asp Gln Lys Glu Glu Val Gln 1 5 10 15 704 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide704 Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu 1 5 1015 705 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 705 Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val GlnLeu Leu 1 5 10 15 706 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 706 Ile Cys Glu Val Glu Asp Gln LysGlu Glu Val Gln Leu Leu Val 1 5 10 15 707 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 707 Cys Glu Val GluAsp Gln Lys Glu Glu Val Gln Leu Leu Val Phe 1 5 10 15 708 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide708 Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly 1 5 1015 709 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 709 Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val PheGly Leu 1 5 10 15 710 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 710 Glu Asp Gln Lys Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr 1 5 10 15 711 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 711 Asp Gln Lys GluGlu Val Gln Leu Leu Val Phe Gly Leu Thr Ala 1 5 10 15 712 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide712 Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn 1 5 1015 713 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 713 Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr AlaAsn Ser 1 5 10 15 714 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 714 Glu Glu Val Gln Leu Leu Val PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 715 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 715 Glu Val Gln LeuLeu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr 1 5 10 15 716 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide716 Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His 1 5 1015 717 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 717 Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp ThrHis Leu 1 5 10 15 718 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 718 Leu Leu Val Phe Gly Leu Thr AlaAsn Ser Asp Thr His Leu Leu 1 5 10 15 719 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 719 Leu Val Phe GlyLeu Thr Ala Asn Ser Asp Thr His Leu Leu Gln 1 5 10 15 720 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide720 Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly 1 5 1015 721 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 721 Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu GlnGly Gln 1 5 10 15 722 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 722 Gly Leu Thr Ala Asn Ser Asp ThrHis Leu Leu Gln Gly Gln Ser 1 5 10 15 723 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 723 Leu Thr Ala AsnSer Asp Thr His Leu Leu Gln Gly Gln Ser Leu 1 5 10 15 724 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide724 Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser Leu Thr 1 5 1015 725 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 725 Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser LeuThr Leu 1 5 10 15 726 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 726 Asn Ser Asp Thr His Leu Leu GlnGly Gln Ser Leu Thr Leu Thr 1 5 10 15 727 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 727 Ser Asp Thr HisLeu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu 1 5 10 15 728 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide728 Asp Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 5 1015 729 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 729 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 730 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 730 His Leu Leu Gln Gly Gln Ser LeuThr Leu Thr Leu Glu Ser Pro 1 5 10 15 731 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 731 Leu Trp Asp GlnGly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile 1 5 10 15 Glu Asp 732 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 732 Trp Asp Gln Gly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys IleGlu 1 5 10 15 Asp Ser 733 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 733 Asp Gln Gly Asn Phe Pro Leu IleIle Lys Asn Leu Lys Ile Glu Asp 1 5 10 15 Ser Asp 734 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 734 Gln GlyAsn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser 1 5 10 15 AspThr 735 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 735 Gly Asn Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile GluAsp Ser Asp 1 5 10 15 Thr Tyr 736 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 736 Asn Phe Pro Leu Ile Ile LysAsn Leu Lys Ile Glu Asp Ser Asp Thr 1 5 10 15 Tyr Ile 737 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide737 Phe Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr 1 510 15 Ile Cys 738 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 738 Pro Leu Ile Ile Lys Asn Leu Lys Ile Glu AspSer Asp Thr Tyr Ile 1 5 10 15 Cys Glu 739 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 739 Leu Ile Ile LysAsn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys 1 5 10 15 Glu Val 740 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 740 Ile Ile Lys Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile CysGlu 1 5 10 15 Val Glu 741 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 741 Ile Lys Asn Leu Lys Ile Glu AspSer Asp Thr Tyr Ile Cys Glu Val 1 5 10 15 Glu Asp 742 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 742 Lys AsnLeu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu 1 5 10 15 AspGln 743 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 743 Asn Leu Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys GluVal Glu Asp 1 5 10 15 Gln Lys 744 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 744 Leu Lys Ile Glu Asp Ser AspThr Tyr Ile Cys Glu Val Glu Asp Gln 1 5 10 15 Lys Glu 745 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide745 Lys Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys 1 510 15 Glu Glu 746 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 746 Ile Glu Asp Ser Asp Thr Tyr Ile Cys Glu ValGlu Asp Gln Lys Glu 1 5 10 15 Glu Val 747 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 747 Glu Asp Ser AspThr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu 1 5 10 15 Val Gln 748 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 748 Asp Ser Asp Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu GluVal 1 5 10 15 Gln Leu 749 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 749 Ser Asp Thr Tyr Ile Cys Glu ValGlu Asp Gln Lys Glu Glu Val Gln 1 5 10 15 Leu Leu 750 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 750 Asp ThrTyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu 1 5 10 15 LeuVal 751 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 751 Thr Tyr Ile Cys Glu Val Glu Asp Gln Lys Glu Glu ValGln Leu Leu 1 5 10 15 Val Phe 752 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 752 Tyr Ile Cys Glu Val Glu AspGln Lys Glu Glu Val Gln Leu Leu Val 1 5 10 15 Phe Gly 753 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide753 Ile Cys Glu Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe 1 510 15 Gly Leu 754 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 754 Cys Glu Val Glu Asp Gln Lys Glu Glu Val GlnLeu Leu Val Phe Gly 1 5 10 15 Leu Thr 755 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 755 Glu Val Glu AspGln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu 1 5 10 15 Thr Ala 756 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 756 Val Glu Asp Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly LeuThr 1 5 10 15 Ala Asn 757 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 757 Glu Asp Gln Lys Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala 1 5 10 15 Asn Ser 758 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 758 Asp GlnLys Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn 1 5 10 15 SerAsp 759 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 759 Gln Lys Glu Glu Val Gln Leu Leu Val Phe Gly Leu ThrAla Asn Ser 1 5 10 15 Asp Thr 760 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 760 Lys Glu Glu Val Gln Leu LeuVal Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 Thr His 761 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide761 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr 1 510 15 His Leu 762 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 762 Glu Val Gln Leu Leu Val Phe Gly Leu Thr AlaAsn Ser Asp Thr His 1 5 10 15 Leu Leu 763 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 763 Val Gln Leu LeuVal Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu 1 5 10 15 Leu Gln 764 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 764 Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His LeuLeu 1 5 10 15 Gln Gly 765 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 765 Leu Leu Val Phe Gly Leu Thr AlaAsn Ser Asp Thr His Leu Leu Gln 1 5 10 15 Gly Gln 766 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 766 Leu ValPhe Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly 1 5 10 15 GlnSer 767 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 767 Val Phe Gly Leu Thr Ala Asn Ser Asp Thr His Leu LeuGln Gly Gln 1 5 10 15 Ser Leu 768 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 768 Phe Gly Leu Thr Ala Asn SerAsp Thr His Leu Leu Gln Gly Gln Ser 1 5 10 15 Leu Thr 769 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide769 Gly Leu Thr Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser Leu 1 510 15 Thr Leu 770 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 770 Leu Thr Ala Asn Ser Asp Thr His Leu Leu GlnGly Gln Ser Leu Thr 1 5 10 15 Leu Thr 771 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 771 Thr Ala Asn SerAsp Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu 1 5 10 15 Thr Leu 772 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 772 Ala Asn Ser Asp Thr His Leu Leu Gln Gly Gln Ser Leu Thr LeuThr 1 5 10 15 Leu Glu 773 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 773 Asn Ser Asp Thr His Leu Leu GlnGly Gln Ser Leu Thr Leu Thr Leu 1 5 10 15 Glu Ser 774 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 774 Ser AspThr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 5 10 15 SerPro 775 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 775 Trp Thr Cys Thr Val Leu Gln Asn Gln Lys Lys Val GluPhe Lys 1 5 10 15 776 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 776 Thr Cys Thr Val Leu Gln Asn GlnLys Lys Val Glu Phe Lys Ile 1 5 10 15 777 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 777 Cys Thr Val LeuGln Asn Gln Lys Lys Val Glu Phe Lys Ile Asp 1 5 10 15 778 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide778 Thr Val Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile 1 5 1015 779 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 779 Val Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile AspIle Val 1 5 10 15 780 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 780 Leu Gln Asn Gln Lys Lys Val GluPhe Lys Ile Asp Ile Val Val 1 5 10 15 781 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 781 Gln Asn Gln LysLys Val Glu Phe Lys Ile Asp Ile Val Val Leu 1 5 10 15 782 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide782 Asn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val Leu Ala 1 5 1015 783 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 783 Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val LeuAla Phe 1 5 10 15 784 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 784 Lys Lys Val Glu Phe Lys Ile AspIle Val Val Leu Ala Phe Gln 1 5 10 15 785 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 785 Lys Val Glu PheLys Ile Asp Ile Val Val Leu Ala Phe Gln Lys 1 5 10 15 786 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide786 Val Glu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala 1 5 1015 787 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 787 Glu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln LysAla Ser 1 5 10 15 788 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 788 Phe Lys Ile Asp Ile Val Val LeuAla Phe Gln Lys Ala Ser Ser 1 5 10 15 789 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 789 Lys Ile Asp IleVal Val Leu Ala Phe Gln Lys Ala Ser Ser Ile 1 5 10 15 790 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide790 Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val 1 5 1015 791 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 791 Asp Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser IleVal Tyr 1 5 10 15 792 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 792 Ile Val Val Leu Ala Phe Gln LysAla Ser Ser Ile Val Tyr Lys 1 5 10 15 793 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 793 Val Val Leu AlaPhe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys 1 5 10 15 794 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide794 Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu 1 5 1015 795 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 795 Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr Lys LysGlu Gly 1 5 10 15 796 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 796 Ala Phe Gln Lys Ala Ser Ser IleVal Tyr Lys Lys Glu Gly Glu 1 5 10 15 797 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 797 Phe Gln Lys AlaSer Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln 1 5 10 15 798 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide798 Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val 1 5 1015 799 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 799 Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu GlnVal Glu 1 5 10 15 800 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 800 Ala Ser Ser Ile Val Tyr Lys LysGlu Gly Glu Gln Val Glu Phe 1 5 10 15 801 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 801 Ser Ser Ile ValTyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser 1 5 10 15 802 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide802 Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe 1 5 1015 803 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 803 Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe SerPhe Pro 1 5 10 15 804 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 804 Val Tyr Lys Lys Glu Gly Glu GlnVal Glu Phe Ser Phe Pro Leu 1 5 10 15 805 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 805 Tyr Lys Lys GluGly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala 1 5 10 15 806 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide806 Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe 1 5 1015 807 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 807 Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu AlaPhe Thr 1 5 10 15 808 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 808 Glu Gly Glu Gln Val Glu Phe SerPhe Pro Leu Ala Phe Thr Val 1 5 10 15 809 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 809 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 810 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide810 Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys 1 5 1015 811 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 811 Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val GluLys Leu 1 5 10 15 812 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 812 Val Glu Phe Ser Phe Pro Leu AlaPhe Thr Val Glu Lys Leu Thr 1 5 10 15 813 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 813 Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly 1 5 10 15 814 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide814 Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser 1 5 1015 815 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 815 Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr GlySer Gly 1 5 10 15 816 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 816 Phe Pro Leu Ala Phe Thr Val GluLys Leu Thr Gly Ser Gly Glu 1 5 10 15 817 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 817 Pro Leu Ala PheThr Val Glu Lys Leu Thr Gly Ser Gly Glu Leu 1 5 10 15 818 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide818 Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu Leu Trp 1 5 1015 819 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 819 Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu LeuTrp Trp 1 5 10 15 820 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 820 Phe Thr Val Glu Lys Leu Thr GlySer Gly Glu Leu Trp Trp Gln 1 5 10 15 821 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 821 Thr Val Glu LysLeu Thr Gly Ser Gly Glu Leu Trp Trp Gln Ala 1 5 10 15 822 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide822 Val Glu Lys Leu Thr Gly Ser Gly Glu Leu Trp Trp Gln Ala Glu 1 5 1015 823 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 823 Glu Lys Leu Thr Gly Ser Gly Glu Leu Trp Trp Gln AlaGlu Arg 1 5 10 15 824 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 824 Trp Thr Cys Thr Val Leu Gln AsnGln Lys Lys Val Glu Phe Lys Ile 1 5 10 15 Asp Ile 825 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 825 Thr CysThr Val Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile Asp 1 5 10 15 IleVal 826 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 826 Cys Thr Val Leu Gln Asn Gln Lys Lys Val Glu Phe LysIle Asp Ile 1 5 10 15 Val Val 827 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 827 Thr Val Leu Gln Asn Gln LysLys Val Glu Phe Lys Ile Asp Ile Val 1 5 10 15 Val Leu 828 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide828 Val Leu Gln Asn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val 1 510 15 Leu Ala 829 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 829 Leu Gln Asn Gln Lys Lys Val Glu Phe Lys IleAsp Ile Val Val Leu 1 5 10 15 Ala Phe 830 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 830 Gln Asn Gln LysLys Val Glu Phe Lys Ile Asp Ile Val Val Leu Ala 1 5 10 15 Phe Gln 831 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 831 Asn Gln Lys Lys Val Glu Phe Lys Ile Asp Ile Val Val Leu AlaPhe 1 5 10 15 Gln Lys 832 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 832 Gln Lys Lys Val Glu Phe Lys IleAsp Ile Val Val Leu Ala Phe Gln 1 5 10 15 Lys Ala 833 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 833 Lys LysVal Glu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln Lys 1 5 10 15 AlaSer 834 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 834 Lys Val Glu Phe Lys Ile Asp Ile Val Val Leu Ala PheGln Lys Ala 1 5 10 15 Ser Ser 835 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 835 Val Glu Phe Lys Ile Asp IleVal Val Leu Ala Phe Gln Lys Ala Ser 1 5 10 15 Ser Ile 836 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide836 Glu Phe Lys Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser 1 510 15 Ile Val 837 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 837 Phe Lys Ile Asp Ile Val Val Leu Ala Phe GlnLys Ala Ser Ser Ile 1 5 10 15 Val Tyr 838 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 838 Lys Ile Asp IleVal Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val 1 5 10 15 Tyr Lys 839 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 839 Ile Asp Ile Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile ValTyr 1 5 10 15 Lys Lys 840 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 840 Asp Ile Val Val Leu Ala Phe GlnLys Ala Ser Ser Ile Val Tyr Lys 1 5 10 15 Lys Glu 841 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 841 Ile ValVal Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys 1 5 10 15 GluGly 842 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 842 Val Val Leu Ala Phe Gln Lys Ala Ser Ser Ile Val TyrLys Lys Glu 1 5 10 15 Gly Glu 843 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 843 Val Leu Ala Phe Gln Lys AlaSer Ser Ile Val Tyr Lys Lys Glu Gly 1 5 10 15 Glu Gln 844 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide844 Leu Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu 1 510 15 Gln Val 845 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 845 Ala Phe Gln Lys Ala Ser Ser Ile Val Tyr LysLys Glu Gly Glu Gln 1 5 10 15 Val Glu 846 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 846 Phe Gln Lys AlaSer Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val 1 5 10 15 Glu Phe 847 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 847 Gln Lys Ala Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln ValGlu 1 5 10 15 Phe Ser 848 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 848 Lys Ala Ser Ser Ile Val Tyr LysLys Glu Gly Glu Gln Val Glu Phe 1 5 10 15 Ser Phe 849 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 849 Ala SerSer Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser 1 5 10 15 PhePro 850 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 850 Ser Ser Ile Val Tyr Lys Lys Glu Gly Glu Gln Val GluPhe Ser Phe 1 5 10 15 Pro Leu 851 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 851 Ser Ile Val Tyr Lys Lys GluGly Glu Gln Val Glu Phe Ser Phe Pro 1 5 10 15 Leu Ala 852 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide852 Ile Val Tyr Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu 1 510 15 Ala Phe 853 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 853 Val Tyr Lys Lys Glu Gly Glu Gln Val Glu PheSer Phe Pro Leu Ala 1 5 10 15 Phe Thr 854 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 854 Tyr Lys Lys GluGly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe 1 5 10 15 Thr Val 855 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 855 Lys Lys Glu Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala PheThr 1 5 10 15 Val Glu 856 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 856 Lys Glu Gly Glu Gln Val Glu PheSer Phe Pro Leu Ala Phe Thr Val 1 5 10 15 Glu Lys 857 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 857 Glu GlyGlu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 LysLeu 858 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 858 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrVal Glu Lys 1 5 10 15 Leu Thr 859 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 859 Glu Gln Val Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu Lys Leu 1 5 10 15 Thr Gly 860 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide860 Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr 1 510 15 Gly Ser 861 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 861 Val Glu Phe Ser Phe Pro Leu Ala Phe Thr ValGlu Lys Leu Thr Gly 1 5 10 15 Ser Gly 862 18 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 862 Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser 1 5 10 15 Gly Glu 863 18PRT Artificial Sequence Description of Artificial Sequence bindingpeptide 863 Phe Ser Phe Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly SerGly 1 5 10 15 Glu Leu 864 18 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 864 Ser Phe Pro Leu Ala Phe Thr ValGlu Lys Leu Thr Gly Ser Gly Glu 1 5 10 15 Leu Trp 865 18 PRT ArtificialSequence Description of Artificial Sequence binding peptide 865 Phe ProLeu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu Leu 1 5 10 15 TrpTrp 866 18 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 866 Pro Leu Ala Phe Thr Val Glu Lys Leu Thr Gly Ser GlyGlu Leu Trp 1 5 10 15 Trp Gln 867 18 PRT Artificial Sequence Descriptionof Artificial Sequence binding peptide 867 Leu Ala Phe Thr Val Glu LysLeu Thr Gly Ser Gly Glu Leu Trp Trp 1 5 10 15 Gln Ala 868 18 PRTArtificial Sequence Description of Artificial Sequence binding peptide868 Ala Phe Thr Val Glu Lys Leu Thr Gly Ser Gly Glu Leu Trp Trp Gln 1 510 15 Ala Glu 869 18 PRT Artificial Sequence Description of ArtificialSequence binding peptide 869 Phe Thr Val Glu Lys Leu Thr Gly Ser Gly GluLeu Trp Trp Gln Ala 1 5 10 15 Glu Arg 870 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 870 Asp Gln Gly AsnPhe Pro Leu Ile Ile 1 5 871 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 871 Gln Gly Asn Phe Pro Leu Ile IleLys 1 5 872 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 872 Gly Asn Phe Pro Leu Ile Ile Lys Asn 1 5 873 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide873 Asn Phe Pro Leu Ile Ile Lys Asn Leu 1 5 874 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 874 Phe ProLeu Ile Ile Lys Asn Leu Lys 1 5 875 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 875 Pro Leu Ile IleLys Asn Leu Lys Ile 1 5 876 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 876 Leu Ile Ile Lys Asn Leu Lys IleGlu 1 5 877 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 877 Ile Ile Lys Asn Leu Lys Ile Glu Asp 1 5 878 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide878 Ile Lys Asn Leu Lys Ile Glu Asp Ser 1 5 879 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 879 Lys AsnLeu Lys Ile Glu Asp Ser Asp 1 5 880 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 880 Asn Leu Lys IleGlu Asp Ser Asp Thr 1 5 881 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 881 Leu Lys Ile Glu Asp Ser Asp ThrTyr 1 5 882 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 882 Lys Ile Glu Asp Ser Asp Thr Tyr Ile 1 5 883 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide883 Ile Glu Asp Ser Asp Thr Tyr Ile Cys 1 5 884 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 884 Glu AspSer Asp Thr Tyr Ile Cys Glu 1 5 885 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 885 Asp Ser Asp ThrTyr Ile Cys Glu Val 1 5 886 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 886 Ser Asp Thr Tyr Ile Cys Glu ValGlu 1 5 887 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 887 Asp Thr Tyr Ile Cys Glu Val Glu Asp 1 5 888 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide888 Thr Tyr Ile Cys Glu Val Glu Asp Gln 1 5 889 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 889 Tyr IleCys Glu Val Glu Asp Gln Lys 1 5 890 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 890 Ile Cys Glu ValGlu Asp Gln Lys Glu 1 5 891 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 891 Cys Glu Val Glu Asp Gln Lys GluGlu 1 5 892 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 892 Glu Val Glu Asp Gln Lys Glu Glu Val 1 5 893 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide893 Val Glu Asp Gln Lys Glu Glu Val Gln 1 5 894 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 894 Glu AspGln Lys Glu Glu Val Gln Leu 1 5 895 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 895 Asp Gln Lys GluGlu Val Gln Leu Leu 1 5 896 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 896 Gln Lys Glu Glu Val Gln Leu LeuVal 1 5 897 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 897 Lys Glu Glu Val Gln Leu Leu Val Phe 1 5 898 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide898 Glu Glu Val Gln Leu Leu Val Phe Gly 1 5 899 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 899 Glu ValGln Leu Leu Val Phe Gly Leu 1 5 900 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 900 Val Gln Leu LeuVal Phe Gly Leu Thr 1 5 901 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 901 Gln Leu Leu Val Phe Gly Leu ThrAla 1 5 902 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 902 Leu Leu Val Phe Gly Leu Thr Ala Asn 1 5 903 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide903 Leu Val Phe Gly Leu Thr Ala Asn Ser 1 5 904 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 904 Val PheGly Leu Thr Ala Asn Ser Asp 1 5 905 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 905 Phe Gly Leu ThrAla Asn Ser Asp Thr 1 5 906 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 906 Gly Leu Thr Ala Asn Ser Asp ThrHis 1 5 907 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 907 Leu Thr Ala Asn Ser Asp Thr His Leu 1 5 908 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide908 Thr Ala Asn Ser Asp Thr His Leu Leu 1 5 909 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 909 Ala AsnSer Asp Thr His Leu Leu Gln 1 5 910 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 910 Asn Ser Asp ThrHis Leu Leu Gln Gly 1 5 911 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 911 Ser Asp Thr His Leu Leu Gln GlyGln 1 5 912 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 912 Asp Thr His Leu Leu Gln Gly Gln Ser 1 5 913 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide913 Thr His Leu Leu Gln Gly Gln Ser Leu 1 5 914 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 914 His LeuLeu Gln Gly Gln Ser Leu Thr 1 5 915 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 915 Leu Leu Gln GlyGln Ser Leu Thr Leu 1 5 916 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 916 Leu Gln Gly Gln Ser Leu Thr LeuThr 1 5 917 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 917 Gln Gly Gln Ser Leu Thr Leu Thr Leu 1 5 918 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide918 Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 5 919 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 919 Asp GlnGly Asn Phe Pro Leu Ile Ile Lys Asn Leu 1 5 10 920 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 920 Gln GlyAsn Phe Pro Leu Ile Ile Lys Asn Leu Lys 1 5 10 921 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 921 Gly AsnPhe Pro Leu Ile Ile Lys Asn Leu Lys Ile 1 5 10 922 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 922 Asn PhePro Leu Ile Ile Lys Asn Leu Lys Ile Glu 1 5 10 923 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 923 Phe ProLeu Ile Ile Lys Asn Leu Lys Ile Glu Asp 1 5 10 924 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 924 Pro LeuIle Ile Lys Asn Leu Lys Ile Glu Asp Ser 1 5 10 925 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 925 Leu IleIle Lys Asn Leu Lys Ile Glu Asp Ser Asp 1 5 10 926 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 926 Ile IleLys Asn Leu Lys Ile Glu Asp Ser Asp Thr 1 5 10 927 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 927 Ile LysAsn Leu Lys Ile Glu Asp Ser Asp Thr Tyr 1 5 10 928 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 928 Lys AsnLeu Lys Ile Glu Asp Ser Asp Thr Tyr Ile 1 5 10 929 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 929 Asn LeuLys Ile Glu Asp Ser Asp Thr Tyr Ile Cys 1 5 10 930 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 930 Leu LysIle Glu Asp Ser Asp Thr Tyr Ile Cys Glu 1 5 10 931 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 931 Lys IleGlu Asp Ser Asp Thr Tyr Ile Cys Glu Val 1 5 10 932 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 932 Ile GluAsp Ser Asp Thr Tyr Ile Cys Glu Val Glu 1 5 10 933 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 933 Glu AspSer Asp Thr Tyr Ile Cys Glu Val Glu Asp 1 5 10 934 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 934 Asp SerAsp Thr Tyr Ile Cys Glu Val Glu Asp Gln 1 5 10 935 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 935 Ser AspThr Tyr Ile Cys Glu Val Glu Asp Gln Lys 1 5 10 936 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 936 Asp ThrTyr Ile Cys Glu Val Glu Asp Gln Lys Glu 1 5 10 937 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 937 Thr TyrIle Cys Glu Val Glu Asp Gln Lys Glu Glu 1 5 10 938 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 938 Tyr IleCys Glu Val Glu Asp Gln Lys Glu Glu Val 1 5 10 939 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 939 Ile CysGlu Val Glu Asp Gln Lys Glu Glu Val Gln 1 5 10 940 11 PRT ArtificialSequence Description of Artificial Sequence binding peptide 940 Cys GluVal Glu Asp Gln Lys Glu Glu Val Gln 1 5 10 941 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 941 Glu ValGlu Asp Gln Lys Glu Glu Val Gln Leu Leu 1 5 10 942 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 942 Val GluAsp Gln Lys Glu Glu Val Gln Leu Leu Val 1 5 10 943 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 943 Glu AspGln Lys Glu Glu Val Gln Leu Leu Val Phe 1 5 10 944 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 944 Asp GlnLys Glu Glu Val Gln Leu Leu Val Phe Gly 1 5 10 945 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 945 Gln LysGlu Glu Val Gln Leu Leu Val Phe Gly Leu 1 5 10 946 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 946 Lys GluGlu Val Gln Leu Leu Val Phe Gly Leu Thr 1 5 10 947 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 947 Glu GluVal Gln Leu Leu Val Phe Gly Leu Thr Ala 1 5 10 948 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 948 Glu ValGln Leu Leu Val Phe Gly Leu Thr Ala Asn 1 5 10 949 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 949 Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser 1 5 10 950 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 950 Gln LeuLeu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 951 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 951 Leu LeuVal Phe Gly Leu Thr Ala Asn Ser Asp Thr 1 5 10 952 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 952 Leu ValPhe Gly Leu Thr Ala Asn Ser Asp Thr His 1 5 10 953 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 953 Val PheGly Leu Thr Ala Asn Ser Asp Thr His Leu 1 5 10 954 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 954 Phe GlyLeu Thr Ala Asn Ser Asp Thr His Leu Leu 1 5 10 955 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 955 Gly LeuThr Ala Asn Ser Asp Thr His Leu Leu Gln 1 5 10 956 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 956 Leu ThrAla Asn Ser Asp Thr His Leu Leu Gln Gly 1 5 10 957 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 957 Thr AlaAsn Ser Asp Thr His Leu Leu Gln Gly Gln 1 5 10 958 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 958 Ala AsnSer Asp Thr His Leu Leu Gln Gly Gln Ser 1 5 10 959 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 959 Asn SerAsp Thr His Leu Leu Gln Gly Gln Ser Leu 1 5 10 960 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 960 Ser AspThr His Leu Leu Gln Gly Gln Ser Leu Thr 1 5 10 961 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 961 Asp ThrHis Leu Leu Gln Gly Gln Ser Leu Thr Leu 1 5 10 962 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 962 Thr HisLeu Leu Gln Gly Gln Ser Leu Thr Leu Thr 1 5 10 963 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 963 His LeuLeu Gln Gly Gln Ser Leu Thr Leu Thr Leu 1 5 10 964 12 PRT ArtificialSequence Description of Artificial Sequence binding peptide 964 Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Leu Glu 1 5 10 965 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 965 Thr ValLeu Gln Asn Gln Lys Lys Val 1 5 966 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 966 Val Leu Gln AsnGln Lys Lys Val Glu 1 5 967 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 967 Leu Gln Asn Gln Lys Lys Val GluPhe 1 5 968 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 968 Gln Asn Gln Lys Lys Val Glu Phe Lys 1 5 969 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide969 Asn Gln Lys Lys Val Glu Phe Lys Ile 1 5 970 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 970 Gln LysLys Val Glu Phe Lys Ile Asp 1 5 971 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 971 Lys Lys Val GluPhe Lys Ile Asp Ile 1 5 972 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 972 Lys Val Glu Phe Lys Ile Asp IleVal 1 5 973 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 973 Val Glu Phe Lys Ile Asp Ile Val Val 1 5 974 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide974 Glu Phe Lys Ile Asp Ile Val Val Leu 1 5 975 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 975 Phe LysIle Asp Ile Val Val Leu Ala 1 5 976 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 976 Lys Ile Asp IleVal Val Leu Ala Phe 1 5 977 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 977 Ile Asp Ile Val Val Leu Ala PheGln 1 5 978 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 978 Asp Ile Val Val Leu Ala Phe Gln Lys 1 5 979 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide979 Ile Val Val Leu Ala Phe Gln Lys Ala 1 5 980 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 980 Val ValLeu Ala Phe Gln Lys Ala Ser 1 5 981 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 981 Val Leu Ala PheGln Lys Ala Ser Ser 1 5 982 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 982 Leu Ala Phe Gln Lys Ala Ser SerIle 1 5 983 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 983 Ala Phe Gln Lys Ala Ser Ser Ile Val 1 5 984 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide984 Phe Gln Lys Ala Ser Ser Ile Val Tyr 1 5 985 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 985 Gln LysAla Ser Ser Ile Val Tyr Lys 1 5 986 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 986 Lys Ala Ser SerIle Val Tyr Lys Lys 1 5 987 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 987 Ala Ser Ser Ile Val Tyr Lys LysGlu 1 5 988 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 988 Ser Ser Ile Val Tyr Lys Lys Glu Gly 1 5 989 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide989 Ser Ile Val Tyr Lys Lys Glu Gly Glu 1 5 990 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 990 Ile ValTyr Lys Lys Glu Gly Glu Gln 1 5 991 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 991 Val Tyr Lys LysGlu Gly Glu Gln Val 1 5 992 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 992 Tyr Lys Lys Glu Gly Glu Gln ValGlu 1 5 993 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 993 Lys Lys Glu Gly Glu Gln Val Glu Phe 1 5 994 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide994 Lys Glu Gly Glu Gln Val Glu Phe Ser 1 5 995 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 995 Glu GlyGlu Gln Val Glu Phe Ser Phe 1 5 996 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 996 Gly Glu Gln ValGlu Phe Ser Phe Pro 1 5 997 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 997 Glu Gln Val Glu Phe Ser Phe ProLeu 1 5 998 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 998 Gln Val Glu Phe Ser Phe Pro Leu Ala 1 5 999 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide999 Val Glu Phe Ser Phe Pro Leu Ala Phe 1 5 1000 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 1000 Glu PheSer Phe Pro Leu Ala Phe Thr 1 5 1001 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1001 Phe Ser Phe ProLeu Ala Phe Thr Val 1 5 1002 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1002 Ser Phe Pro Leu Ala Phe Thr ValGlu 1 5 1003 9 PRT Artificial Sequence Description of ArtificialSequence binding peptide 1003 Phe Pro Leu Ala Phe Thr Val Glu Lys 1 51004 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1004 Pro Leu Ala Phe Thr Val Glu Lys Leu 1 5 1005 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide1005 Leu Ala Phe Thr Val Glu Lys Leu Thr 1 5 1006 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 1006 Ala PheThr Val Glu Lys Leu Thr Gly 1 5 1007 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1007 Phe Thr Val GluLys Leu Thr Gly Ser 1 5 1008 9 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1008 Thr Val Glu Lys Leu Thr Gly SerGly 1 5 1009 9 PRT Artificial Sequence Description of ArtificialSequence binding peptide 1009 Val Glu Lys Leu Thr Gly Ser Gly Glu 1 51010 9 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1010 Glu Lys Leu Thr Gly Ser Gly Glu Leu 1 5 1011 9 PRTArtificial Sequence Description of Artificial Sequence binding peptide1011 Lys Leu Thr Gly Ser Gly Glu Leu Trp 1 5 1012 9 PRT ArtificialSequence Description of Artificial Sequence binding peptide 1012 Leu ThrGly Ser Gly Glu Leu Trp Trp 1 5 1013 9 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1013 Thr Gly Ser GlyGlu Leu Trp Trp Gln 1 5 1014 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1014 Thr Val Leu Gln Asn Gln Lys LysVal Glu Phe Lys 1 5 10 1015 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1015 Val Leu Gln Asn Gln Lys Lys ValGlu Phe Lys Ile 1 5 10 1016 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1016 Leu Gln Asn Gln Lys Lys Val GluPhe Lys Ile Asp 1 5 10 1017 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1017 Gln Asn Gln Lys Lys Val Glu PheLys Ile Asp Ile 1 5 10 1018 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1018 Asn Gln Lys Lys Val Glu Phe LysIle Asp Ile Val 1 5 10 1019 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1019 Gln Lys Lys Val Glu Phe Lys IleAsp Ile Val Val 1 5 10 1020 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1020 Lys Lys Val Glu Phe Lys Ile AspIle Val Val Leu 1 5 10 1021 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1021 Lys Val Glu Phe Lys Ile Asp IleVal Val Leu Ala 1 5 10 1022 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1022 Val Glu Phe Lys Ile Asp Ile ValVal Leu Ala Phe 1 5 10 1023 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1023 Glu Phe Lys Ile Asp Ile Val ValLeu Ala Phe Gln 1 5 10 1024 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1024 Phe Lys Ile Asp Ile Val Val LeuAla Phe Gln Lys 1 5 10 1025 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1025 Lys Ile Asp Ile Val Val Leu AlaPhe Gln Lys Ala 1 5 10 1026 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1026 Ile Asp Ile Val Val Leu Ala PheGln Lys Ala Ser 1 5 10 1027 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1027 Asp Ile Val Val Leu Ala Phe GlnLys Ala Ser Ser 1 5 10 1028 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1028 Ile Val Val Leu Ala Phe Gln LysAla Ser Ser Ile 1 5 10 1029 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1029 Val Val Leu Ala Phe Gln Lys AlaSer Ser Ile Val 1 5 10 1030 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1030 Val Leu Ala Phe Gln Lys Ala SerSer Ile Val Tyr 1 5 10 1031 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1031 Leu Ala Phe Gln Lys Ala Ser SerIle Val Tyr Lys 1 5 10 1032 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1032 Ala Phe Gln Lys Ala Ser Ser IleVal Tyr Lys Lys 1 5 10 1033 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1033 Phe Gln Lys Ala Ser Ser Ile ValTyr Lys Lys Glu 1 5 10 1034 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1034 Gln Lys Ala Ser Ser Ile Val TyrLys Lys Glu Gly 1 5 10 1035 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1035 Lys Ala Ser Ser Ile Val Tyr LysLys Glu Gly Glu 1 5 10 1036 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1036 Ala Ser Ser Ile Val Tyr Lys LysGlu Gly Glu Gln 1 5 10 1037 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1037 Ser Ser Ile Val Tyr Lys Lys GluGly Glu Gln Val 1 5 10 1038 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1038 Ser Ile Val Tyr Lys Lys Glu GlyGlu Gln Val Glu 1 5 10 1039 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1039 Ile Val Tyr Lys Lys Glu Gly GluGln Val Glu Phe 1 5 10 1040 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1040 Val Tyr Lys Lys Glu Gly Glu GlnVal Glu Phe Ser 1 5 10 1041 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1041 Tyr Lys Lys Glu Gly Glu Gln ValGlu Phe Ser Phe 1 5 10 1042 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1042 Lys Lys Glu Gly Glu Gln Val GluPhe Ser Phe Pro 1 5 10 1043 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1043 Lys Glu Gly Glu Gln Val Glu PheSer Phe Pro Leu 1 5 10 1044 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1044 Glu Gly Glu Gln Val Glu Phe SerPhe Pro Leu Ala 1 5 10 1045 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1045 Gly Glu Gln Val Glu Phe Ser PhePro Leu Ala Phe 1 5 10 1046 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1046 Glu Gln Val Glu Phe Ser Phe ProLeu Ala Phe Thr 1 5 10 1047 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1047 Gln Val Glu Phe Ser Phe Pro LeuAla Phe Thr Val 1 5 10 1048 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1048 Val Glu Phe Ser Phe Pro Leu AlaPhe Thr Val Glu 1 5 10 1049 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1049 Glu Phe Ser Phe Pro Leu Ala PheThr Val Glu Lys 1 5 10 1050 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1050 Phe Ser Phe Pro Leu Ala Phe ThrVal Glu Lys Leu 1 5 10 1051 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1051 Ser Phe Pro Leu Ala Phe Thr ValGlu Lys Leu Thr 1 5 10 1052 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1052 Phe Pro Leu Ala Phe Thr Val GluLys Leu Thr Gly 1 5 10 1053 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1053 Pro Leu Ala Phe Thr Val Glu LysLeu Thr Gly Ser 1 5 10 1054 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1054 Leu Ala Phe Thr Val Glu Lys LeuThr Gly Ser Gly 1 5 10 1055 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1055 Ala Phe Thr Val Glu Lys Leu ThrGly Ser Gly Glu 1 5 10 1056 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1056 Phe Thr Val Glu Lys Leu Thr GlySer Gly Glu Leu 1 5 10 1057 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1057 Thr Val Glu Lys Leu Thr Gly SerGly Glu Leu Trp 1 5 10 1058 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1058 Val Glu Lys Leu Thr Gly Ser GlyGlu Leu Trp Trp 1 5 10 1059 12 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1059 Glu Lys Leu Thr Gly Ser Gly GluLeu Trp Trp Gln 1 5 10 1060 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1060 Glx Glx Glx Glx Glx Glx Asp ThrTyr Ile Cys Glu Val Glu Asp 1 5 10 15 1061 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1061 Glx Glx Glx GlxGlx Glx Ala Thr Tyr Ile Cys Glu Val Glu Asp 1 5 10 15 1062 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1062 Glx Glx Glx Glx Glx Glx Asp Ala Tyr Ile Cys Glu Val Glu Asp 1 5 1015 1063 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1063 Glx Glx Glx Glx Glx Glx Asp Thr Ala Ile Cys Glu ValGlu Asp 1 5 10 15 1064 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1064 Glx Glx Glx Glx Glx Glx Asp ThrTyr Ala Cys Glu Val Glu Asp 1 5 10 15 1065 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1065 Glx Glx Glx GlxGlx Glx Asp Thr Tyr Ile Ala Glu Val Glu Asp 1 5 10 15 1066 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1066 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Ala Val Glu Asp 1 5 1015 1067 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1067 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu AlaGlu Asp 1 5 10 15 1068 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1068 Glx Glx Glx Glx Glx Glx Asp ThrTyr Ile Cys Glu Val Ala Asp 1 5 10 15 1069 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1069 Glx Glx Glx GlxGlx Glx Asp Thr Tyr Ile Cys Glu Val Glu Ala 1 5 10 15 1070 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1070 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu Val Glu Asp 1 5 1015 1071 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1071 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu ValGlu Asp 1 5 10 15 1072 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1072 Glx Glx Glx Glx Glx Glx Ala ThrTyr Ile Cys Glu Val Glu Asp 1 5 10 15 1073 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1073 Glx Glx Glx GlxGlx Glx Asp Ala Tyr Ile Cys Glu Val Glu Asp 1 5 10 15 1074 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1074 Glx Glx Glx Glx Glx Glx Asp Thr Ala Ile Cys Glu Val Glu Asp 1 5 1015 1075 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1075 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Ala Glu ValGlu Asp 1 5 10 15 1076 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1076 Glx Glx Glx Glx Glx Glx Asp ThrTyr Ile Cys Ala Val Glu Asp 1 5 10 15 1077 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1077 Glx Glx Glx GlxGlx Glx Asp Thr Tyr Ile Cys Glu Ala Glu Asp 1 5 10 15 1078 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1078 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu Val Ala Asp 1 5 1015 1079 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1079 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu ValGlu Ala 1 5 10 15 1080 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1080 Glx Glx Glx Glx Glx Glx Asp ThrTyr Ile Cys Glu Val Glu Asp 1 5 10 15 1081 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1081 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1082 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1082 Ala Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1083 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1083 Glu Ala Val Gln Leu Leu Val Phe Gly Leu Thr Ala AsnSer Asp 1 5 10 15 1084 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1084 Glu Glu Ala Gln Leu Leu Val PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 1085 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1085 Glu Glu Val AlaLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1086 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1086 Glu Glu Val Gln Ala Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1087 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1087 Glu Glu Val Gln Leu Ala Val Phe Gly Leu Thr Ala AsnSer Asp 1 5 10 15 1088 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1088 Glu Glu Val Gln Leu Leu Ala PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 1089 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1089 Glu Glu Val GlnLeu Leu Val Ala Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1090 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1090 Glu Glu Val Gln Leu Leu Val Phe Ala Leu Thr Ala Asn Ser Asp 1 5 1015 1091 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1091 Glu Glu Val Gln Leu Leu Val Phe Gly Ala Thr Ala AsnSer Asp 1 5 10 15 1092 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1092 Glu Glu Val Gln Leu Leu Val PheGly Leu Ala Ala Asn Ser Asp 1 5 10 15 1093 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1093 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Thr Asn Ser Asp 1 5 10 15 1094 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1094 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Ala Ser Asp 1 5 1015 1095 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1095 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala AsnAla Asp 1 5 10 15 1096 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1096 Glu Glu Val Gln Leu Leu Val PheGly Leu Thr Ala Asn Ser Ala 1 5 10 15 1097 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1097 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1098 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1098 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1099 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1099 Ala Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala AsnSer Asp 1 5 10 15 1100 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1100 Glu Ala Val Gln Leu Leu Val PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 1101 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1101 Glu Glu Ala GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1102 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1102 Glu Glu Val Ala Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1103 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1103 Glu Glu Val Gln Ala Leu Val Phe Gly Leu Thr Ala AsnSer Asp 1 5 10 15 1104 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1104 Glu Glu Val Gln Leu Ala Val PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 1105 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1105 Glu Glu Val GlnLeu Leu Ala Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1106 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1106 Glu Glu Val Gln Leu Leu Val Ala Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1107 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1107 Glu Glu Val Gln Leu Leu Val Phe Ala Leu Thr Ala AsnSer Asp 1 5 10 15 1108 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1108 Glu Glu Val Gln Leu Leu Val PheGly Ala Thr Ala Asn Ser Asp 1 5 10 15 1109 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1109 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Ala Ala Asn Ser Asp 1 5 10 15 1110 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1110 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Thr Asn Ser Asp 1 5 1015 1111 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1111 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala AlaSer Asp 1 5 10 15 1112 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1112 Glu Glu Val Gln Leu Leu Val PheGly Leu Thr Ala Asn Ala Asp 1 5 10 15 1113 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1113 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Ala 1 5 10 15 1114 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1114 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1115 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1115 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1116 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1116 Ala His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1117 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1117 Thr Ala Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 15 1118 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1118 Thr His Ala Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 1015 1119 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1119 Thr His Leu Ala Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1120 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1120 Thr His Leu Leu Ala Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1121 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1121 Thr His Leu LeuGln Ala Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 15 1122 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1122 Thr His Leu Leu Gln Gly Gln Ala Leu Thr Leu Thr Leu Glu Ser 1 5 1015 1123 14 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1123 Thr His Leu Leu Gln Gly Gln Ala Leu Thr Leu Thr LeuGlu 1 5 10 1124 15 PRT Artificial Sequence Description of ArtificialSequence binding peptide 1124 Thr His Leu Leu Gln Gly Gln Ser Ala ThrLeu Thr Leu Glu Ser 1 5 10 15 1125 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1125 Thr His Leu LeuGln Gly Gln Ser Leu Ala Leu Thr Leu Glu Ser 1 5 10 15 1126 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1126 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Ala Thr Leu Glu Ser 1 5 1015 1127 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1127 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Ala LeuGlu Ser 1 5 10 15 1128 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1128 Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Ala Glu Ser 1 5 10 15 1129 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1129 Thr His Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Leu Ala Ser 1 5 10 15 1130 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1130 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ala 1 5 1015 1131 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1131 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1132 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1132 Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1133 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1133 Ala His Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 15 1134 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1134 Thr Ala Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 1015 1135 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1135 Thr His Ala Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1136 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1136 Thr His Leu Ala Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1137 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1137 Thr His Leu LeuAla Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 15 1138 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1138 Thr His Leu Leu Gln Ala Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 1015 1139 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1139 Thr His Leu Leu Gln Gly Ala Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1140 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1140 Thr His Leu Leu Gln Gly Gln AlaLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1141 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1141 Thr His Leu LeuGln Gly Gln Ser Ala Thr Leu Thr Leu Glu Ser 1 5 10 15 1142 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1142 Thr His Leu Leu Gln Gly Gln Ser Leu Ala Leu Thr Leu Glu Ser 1 5 1015 1143 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1143 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Ala Thr LeuGlu Ser 1 5 10 15 1144 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1144 Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Ala Leu Glu Ser 1 5 10 15 1145 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1145 Thr His Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Ala Glu Ser 1 5 10 15 1146 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1146 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Ala Ser 1 5 1015 1147 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1147 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ala 1 5 10 15 1148 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1148 Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1149 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1149 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1150 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1150 Ala Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1151 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1151 Gly Ala Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrVal Glu 1 5 10 15 1152 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1152 Gly Glu Ala Val Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 1153 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1153 Gly Glu Gln AlaGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1154 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1154 Gly Glu Gln Val Ala Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1155 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1155 Gly Glu Gln Val Glu Ala Ser Phe Pro Leu Ala Phe ThrVal Glu 1 5 10 15 1156 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1156 Gly Glu Gln Val Glu Phe Ala PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 1157 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1157 Gly Glu Gln ValGlu Phe Ser Ala Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1158 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1158 Gly Glu Gln Val Glu Phe Ser Phe Ala Leu Ala Phe Thr Val Glu 1 5 1015 1159 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1159 Gly Glu Gln Val Glu Phe Ser Phe Pro Ala Ala Phe ThrVal Glu 1 5 10 15 1160 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1160 Gly Glu Gln Val Glu Phe Ser PhePro Leu Thr Phe Thr Val Glu 1 5 10 15 1161 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1161 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Ala Thr Val Glu 1 5 10 15 1162 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1162 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Ala Val Glu 1 5 1015 1163 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1163 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrAla Glu 1 5 10 15 1164 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1164 Gly Glu Gln Val Glu Phe Ser PhePro Leu Ala Phe Thr Val Ala 1 5 10 15 1165 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1165 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1166 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1166 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1167 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1167 Ala Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrVal Glu 1 5 10 15 1168 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1168 Gly Ala Gln Val Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 1169 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1169 Gly Glu Ala ValGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1170 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1170 Gly Glu Gln Ala Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1171 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1171 Gly Glu Gln Val Ala Phe Ser Phe Pro Leu Ala Phe ThrVal Glu 1 5 10 15 1172 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1172 Gly Glu Gln Val Glu Ala Ser PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 1173 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1173 Gly Glu Gln ValGlu Phe Ala Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1174 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1174 Gly Glu Gln Val Glu Phe Ser Ala Pro Leu Ala Phe Thr Val Glu 1 5 1015 1175 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1175 Gly Glu Gln Val Glu Phe Ser Phe Ala Leu Ala Phe ThrVal Glu 1 5 10 15 1176 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1176 Gly Glu Gln Val Glu Phe Ser PhePro Ala Ala Phe Thr Val Glu 1 5 10 15 1177 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1177 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Thr Phe Thr Val Glu 1 5 10 15 1178 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1178 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Ala Thr Val Glu 1 5 1015 1179 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1179 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe AlaVal Glu 1 5 10 15 1180 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1180 Gly Glu Gln Val Glu Phe Ser PhePro Leu Ala Phe Thr Ala Glu 1 5 10 15 1181 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1181 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Ala 1 5 10 15 1182 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1182 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1183 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1183 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu ValGlu Asp 1 5 10 15 1184 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1184 Glx Glx Glx Glx Glx Glx Asp ThrTyr Ile Cys Glu Val Glu Glx 1 5 10 15 1185 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1185 Glx Glx Glx GlxGlx Glx Asp Thr Tyr Ile Cys Glu Val Glx Glx 1 5 10 15 1186 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1186 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Cys Glu Glx Glx Glx 1 5 1015 1187 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1187 Glx Glx Glx Glx Glx Glx Asp Thr Tyr Ile Glx Glx GlxGlx Glx 1 5 10 15 1188 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1188 Glx Glx Glx Glx Glx Glx Glx ThrTyr Ile Cys Glu Val Glu Asp 1 5 10 15 1189 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1189 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1190 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1190 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Glx 1 5 1015 1191 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1191 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala AsnGlx Glx 1 5 10 15 1192 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1192 Glu Glu Val Gln Leu Leu Val PheGly Leu Thr Ala Glx Glx Glx 1 5 10 15 1193 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1193 Glu Glu Val GlnLeu Leu Val Phe Gly Leu Thr Glx Glx Glx Glx 1 5 10 15 1194 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1194 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Glx Glx Glx Glx Glx 1 5 1015 1195 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1195 Glu Glu Val Gln Leu Leu Val Phe Gly Glx Glx Glx GlxGlx Glx 1 5 10 15 1196 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1196 Glu Glu Val Gln Leu Leu Val PheGlx Glx Glx Glx Glx Glx Glx 1 5 10 15 1197 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1197 Glu Glu Val GlnLeu Leu Val Glx Glx Glx Glx Glx Glx Glx Glx 1 5 10 15 1198 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1198 Glx Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1199 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1199 Glx Glx Val Gln Leu Leu Val Phe Gly Leu Thr Ala AsnSer Asp 1 5 10 15 1200 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1200 Glx Glx Glx Gln Leu Leu Val PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 1201 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1201 Glx Glx Glx GlxLeu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1202 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1202 Glx Glx Glx Glx Glx Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1203 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1203 Glx Glx Glx Glx Glx Glx Val Phe Gly Leu Thr Ala AsnSer Asp 1 5 10 15 1204 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1204 Glx Glx Glx Glx Glx Glx Glx PheGly Leu Thr Ala Asn Ser Asp 1 5 10 15 1205 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1205 Glx Glx Glx GlxGlx Glx Glx Glx Gly Leu Thr Ala Asn Ser Asp 1 5 10 15 1206 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1206 Glu Glu Val Gln Leu Leu Val Phe Gly Leu Thr Ala Asn Ser Asp 1 5 1015 1207 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1207 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1208 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1208 Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Glx 1 5 10 15 1209 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1209 Thr His Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Leu Glx Glx 1 5 10 15 1210 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1210 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Thr Glx Glx Glx 1 5 1015 1211 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1211 Thr His Leu Leu Gln Gly Gln Ser Leu Thr Leu Glx GlxGlx Glx 1 5 10 15 1212 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1212 Thr His Leu Leu Gln Gly Gln SerLeu Thr Glx Glx Glx Glx Glx 1 5 10 15 1213 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1213 Thr His Leu LeuGln Gly Gln Ser Leu Glx Glx Glx Glx Glx Glx 1 5 10 15 1214 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1214 Thr His Leu Leu Gln Gly Gln Ser Glx Glx Glx Glx Glx Glx Glx 1 5 1015 1215 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1215 Thr His Leu Leu Gln Gly Gln Glx Glx Glx Glx Glx GlxGlx Glx 1 5 10 15 1216 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1216 Glx His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1217 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1217 Glx Glx Leu LeuGln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 15 1218 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1218 Glx Glx Glx Leu Gln Gly Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 1015 1219 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1219 Glx Glx Glx Glx Gln Gly Gln Ser Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1220 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1220 Glx Glx Glx Glx Glx Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1221 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1221 Glx Glx Glx GlxGlx Glx Gln Ser Leu Thr Leu Thr Leu Glu Ser 1 5 10 15 1222 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1222 Glx Glx Glx Glx Glx Glx Glx Ser Leu Thr Leu Thr Leu Glu Ser 1 5 1015 1223 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1223 Glx Glx Glx Glx Glx Glx Glx Glx Leu Thr Leu Thr LeuGlu Ser 1 5 10 15 1224 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1224 Thr His Leu Leu Gln Gly Gln SerLeu Thr Leu Thr Leu Glu Ser 1 5 10 15 1225 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1225 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1226 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1226 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glx 1 5 1015 1227 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1227 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrGlx Glx 1 5 10 15 1228 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1228 Gly Glu Gln Val Glu Phe Ser PhePro Leu Ala Phe Glx Glx Glx 1 5 10 15 1229 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1229 Gly Glu Gln ValGlu Phe Ser Phe Pro Leu Ala Glx Glx Glx Glx 1 5 10 15 1230 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1230 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Glx Glx Glx Glx Glx 1 5 1015 1231 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1231 Gly Glu Gln Val Glu Phe Ser Phe Pro Glx Glx Glx GlxGlx Glx 1 5 10 15 1232 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1232 Gly Glu Gln Val Glu Phe Ser PheGlx Glx Glx Glx Glx Glx Glx 1 5 10 15 1233 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1233 Gly Glu Gln ValGlu Phe Ser Glx Glx Glx Glx Glx Glx Glx Glx 1 5 10 15 1234 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1234 Glx Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1235 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1235 Glx Glx Gln Val Glu Phe Ser Phe Pro Leu Ala Phe ThrVal Glu 1 5 10 15 1236 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1236 Glx Glx Glx Val Glu Phe Ser PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 1237 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1237 Glx Glx Glx GlxGlu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1238 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1238 Glx Glx Glx Glx Glx Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015 1239 15 PRT Artificial Sequence Description of Artificial Sequencebinding peptide 1239 Glx Glx Glx Glx Glx Glx Ser Phe Pro Leu Ala Phe ThrVal Glu 1 5 10 15 1240 15 PRT Artificial Sequence Description ofArtificial Sequence binding peptide 1240 Glx Glx Glx Glx Glx Glx Glx PhePro Leu Ala Phe Thr Val Glu 1 5 10 15 1241 15 PRT Artificial SequenceDescription of Artificial Sequence binding peptide 1241 Glx Glx Glx GlxGlx Glx Glx Glx Pro Leu Ala Phe Thr Val Glu 1 5 10 15 1242 15 PRTArtificial Sequence Description of Artificial Sequence binding peptide1242 Gly Glu Gln Val Glu Phe Ser Phe Pro Leu Ala Phe Thr Val Glu 1 5 1015

What is claimed is:
 1. A polypeptide comprising the amino acid sequenceYDIXYYXXE, wherein X is any synthetic or naturally occurring amino acidresidue, such that the polypeptide binds HIV gp120 under physiologicalconditions, and wherein said polypeptide comprises less than about 100contiguous amino acids that are identical to or substantially identicalto the amino acid sequence of the human CCR5 chemokine receptor.
 2. Thepolypeptide of claim 1, which comprises less than about 50 contiguousamino acids that are identical to or substantially identical to theamino acid sequence of the human CCR5 chemokine receptor.
 3. Thepolypeptide of claim 2, which comprises less than about 25 contiguousamino acids that are identical to or substantially identical to theamino acid sequence of the human CCR5 chemokine receptor.
 4. Thepolypeptide of claim 3, which comprises less than about 13 amino acidsthat are identical to or substantially identical to the amino acidsequence of the human CCR5 chemokine receptor.
 5. The polypeptide ofclaim 4, which consists essentially of YDIXYYXXE.
 6. The polypeptide ofany of claims 1-5, which comprises the amino acid sequence YDIN*YYT*S*E,wherein N* is asparaginyl or a synthetic or naturally occurringsubstitute therefor, T* is threoninyl or a synthetic or naturallyoccurring substitute therefor, and S* is serinyl or a synthetic ornaturally occurring substitute therefor.
 7. The polypeptide of claim 6,wherein N* is asparaginyl, T* is threoninyl, and S* is serinyl.
 8. Thepolypeptide of any of claims 1-6, comprising the amino acid sequenceM*D*YQ*V*S*SP*IYDIN*YYT*S*E, wherein each letter indicates the standardamino acid residue designated by that letter, and a letter followeddirectly by an * indicates that any synthetic or naturally occurringamino acid can occupy that position.
 9. The polypeptide of claim 8,wherein said letter followed directly by an * indicates the amino acidresidue represented by the letter or a synthetic or naturally occurringconservative or neutral amino acid substitution therefor.
 10. Thepolypeptide of claim 9, wherein said amino acid sequence isMDYQVSSPIYDINYYTSE.
 11. A polypeptide comprising the amino acid sequenceXEXIXIYXXXNYXXX, wherein X is any synthetic or naturally occurring aminoacid, such that the polypeptide binds HIV gp120 under physiologicalconditions, and wherein said polypeptide less than about 100 contiguousamino acids that are identical to or substantially identical to theamino acid sequence of the human CXCR4 chemokine receptor.
 12. Thepolypeptide of claim 11, which comprises less than about 50 contiguousamino acids that are identical to or substantially identical to theamino acid sequence of the human CXCR4 chemokine receptor.
 13. Thepolypeptide of claim 11, which comprises less than 25 contigous aminoacids that are identical to or substantially identical to the amino acidsequence of the human CXCR4 chemokine receptor.
 14. The polypeptide ofclaim 13, which consists essentially of EXIXIYXXXNY.
 15. The polypeptideof any of claims 11-14, which comprises the amino acid sequenceM*EG*IS*IYT*S*D*NYT*E*E*, wherein each letter indicates the standardamino acid residue designated by that letter, and each letter followeddirectly by an * indicates the amino acid residue represented by theletter or a synthetic or naturally occurring conservative or neutralamino acid substitution therefor.
 16. The polypeptide of claim 15,wherein said amino acid sequence M*EG*IS*IYT*S*D*NYT*E*E* isM*EGISIYTSDNYT*E*E*.
 17. A polypeptide comprising the amino acidsequence EHQAFLQFS, such that the polypeptide binds with HIV gp120 underphysiological conditions and wherein said polypeptide comprises lessthan about 100 contiguous amino acids that are identical to orsubstantially identical to the amino acid sequence of the human STRL33chemokine receptor.
 18. The polypeptide of claim 17, which comprisesless than about 50 contiguous amino acid that are identical to orsubstantially identical to the amino acid sequence of the human STRL33chemokine receptor.
 19. The polypeptide of claim 18, which comprisesless than about 25 contiguous amino acids that are identical to orsubstantially identical to the amino acid sequence of the human STRL33chemokine receptor.
 20. The polypeptide of claim 19, which consistsessentially of the sequence EHQAFLQFS.
 21. A polypeptide comprising atleast a portion or all of an amino acid sequence selected from the groupconsisting of LPPLYSLVFIFGFVGNML, QWDFGNTMCQLLTGLYFIGFFS,SQYQFWKNFQTLKIVILG, APYNIVLLLNTFQEFFGLNNCS, and YAFVGEKFRNYLLVFFQK,wherein the polypeptide binds with HIV gp120 under physiologicalconditions and comprises less than about 100 amino acid residues thatare identical to or substantially identical to the amino acid sequenceof the human CCR5 chemokine receptor.
 22. A polypeptide comprising atleast a portion or all of an amino acid sequence selected from the groupconsisting of LLLTIPDFIFANVSEADD (165-182), VVFQFQHIMVGLILPGIV(197-214), and IDSFILLEIIKQGCEFEN (261-278), wherein the polypeptidebinds with HIV gp120 under physiological conditions and comprises lessthan about 100 amino acid residues that are identical to orsubstantially identical to the amino acid sequence of the human CXCR4chemokine receptor.
 23. A polypeptide comprising at least a portion orall of an amino acid sequence selected from the group consisting ofLVISIFYHKLQSLTDVFL (53-70), PFWAYAGIHEWVFGQVMC (85-102),EAISTVVLATQMTLGFFL (185-202), LTMIVCYSVIIKTLLHAG (205-222),MAVFLLTQMPFNLMKFIRSTHW (237-258), HWEYYAMTSFHYTIMVTE (257-274),ACLNPVLYAFVSLKFRKN (281-298) and SKTFSASHNVEATSMFQL (325-342), whereinthe polypeptide binds with-HIV gp120 under physiological conditions andcomprises less than about 100 amino acid residues that are identical toor substantially identical to the amino acid sequence of the humanSTRL33 chemokine receptor.
 24. A polypeptide comprising at least aportion of or all of an amino acid sequence selected from the groupconsisting of DTYICEVED, EEVQLLVFGLTANSD, THLLQGQSLTLTLES, andGEQVEFSFPLAFTVE, wherein the polypeptide binds with HIV gp120 underphysiological conditions and wherein the polypeptide comprises less thanabout 100 amino acids that are identical to or substantially identicalto the amino acid sequence of the human CD4 cell-surface protein.
 25. Apolypeptide of any of claims 21-24, which comprises all of the aminoacid sequence and 0 to about 6 conservative or neutral amino acidsubstitutions.
 26. The polypeptide of claim 25, comprising 0 amino acidsubstitutions.
 27. The polypeptide of any of claims 21-26, whichcomprises less than about 50 amino acids that are identical to orsubstantially identical to a protein that naturally has the amino acidsequence.
 28. The polypeptide of any of claims 21-26, which comprisesless than about 25 amino acids that are identical to or substantiallyidentical to a protein that naturally has the amino acid sequence. 29.The polypeptide of any of claims 1-28, wherein said polypeptide furthercomprises a pharmaceutically acceptable substituent.
 30. A compositioncomprising the polypeptide of any of claims 1-28, and a carrier.
 31. Anucleic acid encoding the polypeptide of any of claims 1-28, whereinsaid nucleic acid can be expressed in a cell.
 32. The nucleic acid ofclaim 31, further comprising a nucleic acid sequence that encodes asignal sequence, wherein said signal sequence is translated as a fusionprotein with the polypeptide to form a signal sequence-polypeptidefusion, and wherein said signal sequence can cause secretion of at leastthe polypeptide out of a cell in which the nucleic acid is expressed.33. A vector comprising the nucleic acid of claim 31 or
 32. 34. A methodof making an antibody, which method comprises administering animmunogenic amount of a polypeptide of any of claims 1-28 or a nucleicacid of any of claims 31 or 33 to an animal.
 35. A method ofprophylactically or therapeutically treating HIV infection in a mammalin need thereof, which method comprises administering to said mammal aneffective amount of a polypeptide of any of claims 1-28, a nucleic acidof any of claims 31-33, or an anti-antibody to a polypeptide of any ofclaims 1-28.
 36. A method of making an antibody that binds to a gp120envelope protein of a human immunodeficiency virus-1 (HIV-1), saidmethod comprising: (a) labeling a polypeptide of any of claims 1-28 toobtain a labeled compound, (b) providing a library of syntheticpeptides, wherein said library consists of a multiplicity ofsynthetically-produced polypeptides that are homologous to a continuousregion of an HIV-1 gp120 envelope protein, wherein each polypeptide ofsaid library is substantially isolated from every other polypeptide ofsaid library and is located in a known position, (c) individuallycontacting each polypeptide with said labeled compound such that aportion of the labeled compound can bind with the polypeptide, therebyproducing a bound population of each polypeptide and an unboundpopulation of each polypeptide, (d) removing substantially all of theunbound labeled compound from the position occupied by each polypeptide,(e) measuring the amount of labeled compound that remains co-localizedwith each polypeptide, to determine the quantity of labeled compoundbound by each polypeptide, (f) evaluating the amount of labeled compoundbound by each polypeptide to identify a portion of the HIV-1 gp120envelope protein that binds to an (HIV-1)-receptor selected from thegroup consisting of CCR5, CXCR4, STRL33, and CD4, (g) providing animmunizing compound comprising a polypeptide comprising an amino acidsequence that is homologous to said portion of the HIV-1 gp120 envelopeprotein, (h) inserting an immunogenic quantity of said immunizingcompound into an animal to cause said animal to produce an antibody thatbinds with said portion of the HIV-1 gp120 envelope protein.
 37. Themethod of claim 36, wherein said labeled compound comprises a moietyselected from the group consisting of a radioactive atom, an enzyme, apolyhistidinyl moiety, and an antigen that is specifically recognized bya standard antibody.
 38. The method of claim 36 or 37, wherein saidlibrary consists of a multiplicity of synthetically-producedpolypeptides that are identical to a continuous region of an HIV-1 gp120envelope protein.
 39. The method of any of claims 36-38, wherein saidpolypeptides contain at least about 6 amino acid residues and no morethan about 45 amino acid residues.
 40. The method of claim 39, whereinsaid polypeptides contain no more than about 30 amino acid residues. 41.The method of any of claims 36-40, wherein said library comprises amultiplicity of polypeptides of identical lengths.
 42. The method of anyof claims 36-41, wherein said library comprises a multiplicity ofpolypeptides that are homologous to a region of the HIV-1 gp120 envelopeprotein and have an offset of n amino acid residues, wherein n is aninteger of at least 1 and is not greater than the product of length ofthe longest polypeptide measured in amino acid residues and 1.5.
 43. Themethod of claim 42, wherein said offset is not greater than the productof length of the longest polypeptide measured in amino acid residues and1.0.
 44. The method of claim 42, wherein said offset is not greater thanthe product of length of the longest polypeptide measured in amino acidresidues and 0.5.
 45. The method of claim 42, wherein said offset is notgreater than
 30. 46. The method of claim 42, wherein said offset is notgreater than
 15. 47. The method of claim 42, wherein said offset is notgreater than
 4. 48. The method of any of claims 36-47, wherein eachpolypeptide is bound to a solid support and is located in a vessel thatenables each polypeptide to be covered in a liquid that does not contactany other oligonucleotide of the library.
 49. The method of claim 48,wherein each polypeptide is bound to a bead in a vessel or is bound tothe well of a multi-well assay plate.
 50. The method of claim 36,wherein said step of removing substantially all of the unbound labeledcompound comprises the additional steps of (i) removing a liquidcontaining said unbound labeled compound from a solid substrate to whichan polypeptide of the library is bound, (ii) applying a quantity ofwash-liquid to said solid substrate that is sufficient to cover anyportion of said solid substrate or a vessel containing said solidsubstrate that has been contacted by said labeled compound, and (iii)removing said wash-liquid.
 51. The method of any of claims 36-50,wherein said immunizing compound comprises an adjuvant or wherein saidpolypeptide comprising an amino acid sequence that is homologous to saidportion of the HIV gp120 envelope protein is conjugated to a knownimmunogen.
 52. The method of any of claims 36-51, wherein said method isperformed in a mammal belonging to a group selected from the groupconsisting of rodents, canines, felines, and ruminants.
 53. Theimmunizing compound of step (g) of the method of any of claims 36-52.54. An antibody produced by the method of any of claims 36-53.
 55. Amethod of removing HIV from a bodily fluid of a mammal, which methodcomprises extra-corporeally contacting said bodily fluid with a solidsupport to which is attached a polypeptide of any of claims 1-28 or ananti-antibody to a polypeptide of any of claims 1-78, or the antibody ofclaim 54.